+publisher:"Penn State University" +contributor:("Judith S Bond, Committee Chair/Co-Chair")

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Penn State University

1. Keiffer, Timothy. Meprin Metalloproteases Cleave and Inactivate Interleukin-6 .

Degree: 2012, Penn State University

URL: https://submit-etda.libraries.psu.edu/catalog/12674

► The inflammatory response is influenced in part by a class of small molecular-weight proteins called cytokines. There is a complex and changing mixture of cytokines… (more)

▼ The inflammatory response is influenced in part by a class of small molecular-weight proteins called cytokines. There is a complex and changing mixture of cytokines at the sites of inflammation during every stage of the inflammatory process, from initiation to resolution. Proteases can influence the inflammatory response by altering cytokine bio-activity, either through inactivating the cytokine via degradation or activating the cytokine by converting the cytokine from a “pro” form to an active form. Meprins are zinc metalloproteinases of the metzincin superfamily that are comprised of α and/or β subunits that interact with each other to form unique membrane-bound and secreted isoforms. Meprins are expressed in the brush-border membranes of kidney and intestinal epithelial cells along with the epidermal layers of the skin and certain populations of leukocytes. The meprin metalloproteinases have been implicated in the pathogenesis of several inflammatory diseases. It is hypothesized that one mechanism by which meprins modulate and regulate inflammation is by direct proteolytic action on pericellular inflammatory mediators such as cytokines. Interleukin-6 (IL-6) is an important pro-inflammatory mediator and several lines of in vivo data indicate that IL-6 is an in vivo substrate for meprins. The current work focused mainly on characterizing the interaction between meprins and interleukin-6, with the hypothesis that meprins cleave and bio-inactivate IL-6. This work demonstrates that the homomeric isoforms of meprin A and B cleave IL-6 at the C-terminus and remove a five amino acid segment, thereby inactivating the cytokine. Both the homomeric human meprin isoforms and the rodent meprin isoforms cleave human and mouse isoforms of IL-6, thereby decreasing the bio-activity of IL-6. Furthermore, IL-6 inactivated by meprin A or B does not act in an antagonistic manner towards intact IL-6. The homomeric rodent meprin A and B isoforms of meprins cleave human IL-6 with high affinity (apparent) (Km) and efficiency (kcat/Km) values; 4.9 µM and 0.20 µM-1s-1, and 12.0 µM and 2.5 µM-1s-1 for meprin A and B, respectively. Madin-Darby Canine Kidney Cells transiently transfected with meprin β and transfected with either meprin β or meprin α constructs cleave human IL-6. The kinetics of meprin cleavage of IL-6 and the finding that meprins cleave IL-6 in a cell-based system indicate that IL-6 is a good substrate for both meprin A and B and provide a kinetics-based rationale for proposing that meprins are capable of cleaving IL-6 in vivo. While evaluating the interaction between meprins and IL-6 was the main aim of this thesis work, another aim was to study the interaction of endogenous inhibitors with meprins. Endogenous proteinase inhibitors, such as alpha-2-macroglobulin and Tissue Inhibitors of Metalloproteinases (TIMPs), are important for the regulation of some protease activity in vivo, however, they do not inhibit meprin activity. It has been proposed that mannose binding lectin (MBL), which is also… Advisors/Committee Members: Judith S Bond, Dissertation Advisor/Co-Advisor, Chair%22%29&pagesize-30">Judith S Bond, Committee Chair/Co-Chair, Channe D Gowda, Committee Member, Christopher Charles Norbury, Committee Member, Ira Joseph Ropson, Committee Member, Cara Lynne Schengrund, Committee Member, Gavin Peter Robertson, Committee Member.

Subjects/Keywords: Meprin; Interleukin-6; Inflammatory Bowel Disease; Mannose Binding Lectin; Wound Healing

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APA (6^th Edition):

Keiffer, T. (2012). Meprin Metalloproteases Cleave and Inactivate Interleukin-6 . (Thesis). Penn State University. Retrieved from https://submit-etda.libraries.psu.edu/catalog/12674

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Keiffer, Timothy. “Meprin Metalloproteases Cleave and Inactivate Interleukin-6 .” 2012. Thesis, Penn State University. Accessed March 03, 2021. https://submit-etda.libraries.psu.edu/catalog/12674.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Keiffer, Timothy. “Meprin Metalloproteases Cleave and Inactivate Interleukin-6 .” 2012. Web. 03 Mar 2021.

Vancouver:

Keiffer T. Meprin Metalloproteases Cleave and Inactivate Interleukin-6 . [Internet] [Thesis]. Penn State University; 2012. [cited 2021 Mar 03]. Available from: https://submit-etda.libraries.psu.edu/catalog/12674.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Keiffer T. Meprin Metalloproteases Cleave and Inactivate Interleukin-6 . [Thesis]. Penn State University; 2012. Available from: https://submit-etda.libraries.psu.edu/catalog/12674

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Penn State University

2. Yura, Renee E. MEPRIN METALLOPROTEASES MODULATE THE HOST RESPONSE TO ESCHERICHIA COLI .

Degree: 2008, Penn State University

URL: https://submit-etda.libraries.psu.edu/catalog/8602

► Meprin metalloproteases, composed of alpha and/or beta subunits, consist of membrane-bound and secreted forms that are abundantly expressed in kidney and intestinal epithelial cells. They… (more)

▼ Meprin metalloproteases, composed of alpha and/or beta subunits, consist of membrane-bound and secreted forms that are abundantly expressed in kidney and intestinal epithelial cells. They are also expressed in the skin and in certain populations of leukocytes. Meprins have been implicated in several inflammatory diseases, such as renal ischemia, diabetic nephropathy, and inflammatory bowel disease, indicating a role for these enzymes in modulation of the immune response. Prior to the initiation of this work, extensive information about the structure and in vitro behavior of the meprins was known, but little was known about their in vivo roles in immune modulation. These studies are the first to demonstrate a relationship between the inflammatory response and the meprins in both systemic and bladder challenge models. The aim of this work was to determine the role of meprins in the host response to gram-negative uropathic Escherichia coli (E. coli). Initial studies demonstrated marked increases in meprin alpha expression in the urine of women with active urinary tract infections (UTIs), implicating meprin involvement in the host response to bacterial infections. To examine further the role of meprins in the host response to UTI, meprin alpha knockout (alphaKO) and wild-type (WT) mice were challenged with a transurethral inoculation of uropathic E. coli. In this localized model of inflammation, bladder myeloperoxidase (MPO) activity, bladder weight, and bladder permeability were significantly less in alphaKO compared to WT mice after induction of UTI. These data indicate that meprin A is pro-inflammatory, contributing to leukocyte infiltration, edema, and epithelial damage. To determine whether the action of meprin A was the result of a direct interaction with E. coli, extensive in vitro studies were carried out. Meprin A did not decrease the binding of E. coli to bladder cells in culture, nor did it degrade the pili that are responsible for the attachment of E. coli to the bladder epithelium. No evidence of direct interactions between meprin A and E. coli has been found, indicating that the differential response observed in meprin alphaKO mice in comparison to WT is indirect and likely involves the immune system. A large component of the immune response to E. coli is directed toward lipopolysaccharide (LPS) in the bacterial cell wall. Therefore, the responses of meprin alphaKO, meprin beta knockout (betaKO), meprin alphabeta double knockout (alphabetaKO), and WT mice after intraperitoneal (i.p.) LPS challenge were examined. Genotype-specific differences in response to LPS were observed as early as 1 h after challenge with 2.5 mg/kg i.p. E. coli LPS. Meprin alphaKO mice displayed a decreased systemic response to LPS compared to WT mice and meprin betaKO mice, as indicated by lower blood urea nitrogen (BUN) levels, lower serum TNFalpha levels, and less severe hypothermia, implicating meprin in modulation of the host immune response to endotoxin. These data are consistent with those from UTI studies,… Advisors/Committee Members: Chair%22%29&pagesize-30">Judith S Bond, Committee Chair/Co-Chair, Sarah Bronson, Committee Member, Robert G Levenson, Committee Member, Andrea Manni, Committee Member, W. Brian Reeves, Committee Member.

Subjects/Keywords: meprins; metalloproteases; lipopolysaccharide; urinary tract infection; transgenic mouse models

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APA (6^th Edition):

Yura, R. E. (2008). MEPRIN METALLOPROTEASES MODULATE THE HOST RESPONSE TO ESCHERICHIA COLI . (Thesis). Penn State University. Retrieved from https://submit-etda.libraries.psu.edu/catalog/8602

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Yura, Renee E. “MEPRIN METALLOPROTEASES MODULATE THE HOST RESPONSE TO ESCHERICHIA COLI .” 2008. Thesis, Penn State University. Accessed March 03, 2021. https://submit-etda.libraries.psu.edu/catalog/8602.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Yura, Renee E. “MEPRIN METALLOPROTEASES MODULATE THE HOST RESPONSE TO ESCHERICHIA COLI .” 2008. Web. 03 Mar 2021.

Vancouver:

Yura RE. MEPRIN METALLOPROTEASES MODULATE THE HOST RESPONSE TO ESCHERICHIA COLI . [Internet] [Thesis]. Penn State University; 2008. [cited 2021 Mar 03]. Available from: https://submit-etda.libraries.psu.edu/catalog/8602.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Yura RE. MEPRIN METALLOPROTEASES MODULATE THE HOST RESPONSE TO ESCHERICHIA COLI . [Thesis]. Penn State University; 2008. Available from: https://submit-etda.libraries.psu.edu/catalog/8602

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Penn State University

3. BANERJEE, SANJITA. MEPRIN METALLOPROTEASES MODULATE INTESTINAL HOST RESPONSE .

Degree: 2008, Penn State University

URL: https://submit-etda.libraries.psu.edu/catalog/8216

► Meprins, zinc metalloproteases of the astacin family, are composed of two independently expressed subunits meprin alpha and beta which associate to form homo and heter-oligomers,… (more)

▼ Meprins, zinc metalloproteases of the astacin family, are composed of two independently expressed subunits meprin alpha and beta which associate to form homo and heter-oligomers, termed meprin A and B. Meprin isoforms are enriched in human as well as rodent intestine. They have also been reported in kidney, leukocytes, lung and skin. Considerable research has been conducted regarding the in vitro functions of these proteases, however the physiological roles of these proteases are unknown. Generation of meprin beta, alpha and alpha-beta knock-out mice were steps towards filling this void. This work reports the general characterization of the meprin alpha knock-out mouse and investigates the role of meprin proteases in the mouse intestine using a model of colitis. Several polymorphisms have been identified in the human meprin alpha gene that significantly correlate with ulcerative colitis and Crohn’s disease, which make this mouse model relevant to the human pathology. Human and rodent intestines have high but non-uniform meprin expression and hence allow one to study the contributions of different meprin isoforms. To understand the role of meprin A, colitis was induced in wild-type and meprin alpha knock-out mice by dextran sulfate sodium administration. Meprin alpha knock-out mice showed greater susceptibility to injury and had a phenotype of heightened inflammation as evidenced by different markers of inflammation at macroscopic as well as molecular level. Further investigations showed a role for mucosal meprin A in the process of tissue repair. To understand the phenotype of increased inflammation, meprin interaction with immune-mediators was studied at greater detail. This led to the first known documentation of an in vivo interaction of meprins with an immune-mediator, interleukin–18. Subsequent experiments using meprin alpha-beta knock-out mice elucidated the contribution of meprin B in the phenotype in this model of inflammatory bowel disease. These experiments collectively demonstrated a novel function of meprins in immuno-modulation. This thesis furthers our knowledge about the roles of meprin metalloproteases in the rodent intestine and also elucidates the importance of proper distribution of meprin isoforms. Advisors/Committee Members: Chair%22%29&pagesize-30">Judith S Bond, Committee Chair/Co-Chair, Kristin Ann Eckert, Committee Member, Sergei A Grigoryev, Committee Member, Harriet C Isom, Committee Member, Cara Lynne Schengrund, Committee Member.

Subjects/Keywords: MEPRIN; INFLAMMATORY BOWEL DISEASE

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

BANERJEE, S. (2008). MEPRIN METALLOPROTEASES MODULATE INTESTINAL HOST RESPONSE . (Thesis). Penn State University. Retrieved from https://submit-etda.libraries.psu.edu/catalog/8216

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

BANERJEE, SANJITA. “MEPRIN METALLOPROTEASES MODULATE INTESTINAL HOST RESPONSE .” 2008. Thesis, Penn State University. Accessed March 03, 2021. https://submit-etda.libraries.psu.edu/catalog/8216.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

BANERJEE, SANJITA. “MEPRIN METALLOPROTEASES MODULATE INTESTINAL HOST RESPONSE .” 2008. Web. 03 Mar 2021.

Vancouver:

BANERJEE S. MEPRIN METALLOPROTEASES MODULATE INTESTINAL HOST RESPONSE . [Internet] [Thesis]. Penn State University; 2008. [cited 2021 Mar 03]. Available from: https://submit-etda.libraries.psu.edu/catalog/8216.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

BANERJEE S. MEPRIN METALLOPROTEASES MODULATE INTESTINAL HOST RESPONSE . [Thesis]. Penn State University; 2008. Available from: https://submit-etda.libraries.psu.edu/catalog/8216

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Penn State University

4. Ishmael, Susan Senchak. Meprin A Oligomerization: Contributions of N-linked Glycosylation and the MAM Domain .

Degree: 2008, Penn State University

URL: https://submit-etda.libraries.psu.edu/catalog/6899

► The oligomerization of proteins can serve to activate or inhibit functional properties of the proteins, create new functions of the oligomeric complex based on subunit… (more)

▼ The oligomerization of proteins can serve to activate or inhibit functional properties of the proteins, create new functions of the oligomeric complex based on subunit composition, concentrate enzymatic activity, and localize the proteins to a particular region of the cell or extracellular space. Meprins are zinc metalloproteases of the astacin family and metzincin superfamily that are obligate oligomers, targeted to the cell surface of brush border epithelial cells in the kidney and intestine, as well as to the surface of certain leukocytes and cancer cell lines. Meprins are composed of two related subunits, alpha and beta. Depending on the subunit composition, the meprin oligomers range in size from a membrane-bound, disulfide-bonded dimer (homooligomeric meprin B), to tetramers of heterooligomeric meprin A, to large, secreted alpha oligomers of ten or more subunits (homooligomeric meprin A). The work herein investigated the contributions of N-linked glycosylation and the MAM (meprin, A5 protein, protein tyrosine phosphatase μ) domain to the formation and activity of the meprin A homooligomer. Meprins are highly glycosylated, with carbohydrate accounting for approximately 20% of the subunit molecular mass. Using chemical deglycosylation and electrospray mass spectrometry (ESI/MS), it was shown that at least seven of the ten potential N-linked glycosylation sites of mouse meprin A are glycosylated. The glycans are mainly composed of N-acetylglucosamine (GlcNAc), mannose, galactose, and a small amount of fucose. Three glycosylation sites, N234 and N270 in the protease domain and N452 in the TRAF (tumor necrosis factor receptor associated factor) domain, were found to be removed by PNGaseF under native conditions. Removing these glycans did not markedly affect the protein conformation or oligomeric state, but decreased the stability of the oligomer as assessed by urea and heat denaturation. A series of single and double glycosylation site mutants were used to determine the contribution of glycosylation to the formation of the meprin oligomer. No one individual glycosylation site affected formation of the oligomer, although one glycosylation site (N41) influenced the amount of secreted protein in the cell culture system. Interestingly, two protease domain glycosylation sites (N152 and N270) were implicated in oligomerization. The N152Q/N270Q and N152Q/N234Q/N270Q mutants were greatly impaired in their ability to form not only the high molecular mass oligomers, but also the disulfide-bonded dimers. These mutations, unlike the other single and double mutants examined, did not retain proteolytic activity, demonstrating that glycosylation of the protease domain is involved in correct tertiary and quaternary structure formation. The noncatalytic domains of meprin, MAM and TRAF, have previously been shown to contribute to oligomerization of meprin A. Here, a series of single point mutants at charged residues in the putative MAM noncovalent interface (K352G, K361Y, R369Q, R376E, D377Y, D378T, R384G, K388L)… Advisors/Committee Members: Chair%22%29&pagesize-30">Judith S Bond, Committee Chair/Co-Chair, Chair%22%29&pagesize-30">A Daniel Jones, Committee Chair/Co-Chair, Channe D Gowda, Committee Member, Ira Joseph Ropson, Committee Member, Juliette T Lecomte, Committee Member.

Subjects/Keywords: posttranslational modifications; glycosylation; oligomerization; meprins; proteases; MAM domains

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APA (6^th Edition):

Ishmael, S. S. (2008). Meprin A Oligomerization: Contributions of N-linked Glycosylation and the MAM Domain . (Thesis). Penn State University. Retrieved from https://submit-etda.libraries.psu.edu/catalog/6899

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Ishmael, Susan Senchak. “Meprin A Oligomerization: Contributions of N-linked Glycosylation and the MAM Domain .” 2008. Thesis, Penn State University. Accessed March 03, 2021. https://submit-etda.libraries.psu.edu/catalog/6899.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Ishmael, Susan Senchak. “Meprin A Oligomerization: Contributions of N-linked Glycosylation and the MAM Domain .” 2008. Web. 03 Mar 2021.

Vancouver:

Ishmael SS. Meprin A Oligomerization: Contributions of N-linked Glycosylation and the MAM Domain . [Internet] [Thesis]. Penn State University; 2008. [cited 2021 Mar 03]. Available from: https://submit-etda.libraries.psu.edu/catalog/6899.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Ishmael SS. Meprin A Oligomerization: Contributions of N-linked Glycosylation and the MAM Domain . [Thesis]. Penn State University; 2008. Available from: https://submit-etda.libraries.psu.edu/catalog/6899

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Penn State University

5. Tadagavadi, Raghu Kempegowda. Dendritic cells and IL-10 in nephrotoxic acute kidney injury .

Degree: 2009, Penn State University

URL: https://submit-etda.libraries.psu.edu/catalog/10292

► Cisplatin is a highly effective chemotherapeutic agent used to treat a wide variety of tumors in humans. The key limitation with cisplatin therapy is nephrotoxicty… (more)

▼ Cisplatin is a highly effective chemotherapeutic agent used to treat a wide variety of tumors in humans. The key limitation with cisplatin therapy is nephrotoxicty affecting 25-35% of treated patients. Here we investigated the distribution of dendritic cells within the kidney and the role of dendritic cells and dendritic cell-produced IL-10 in cisplatin-induced acute kidney injury using a mouse model in which dendritic cells express green fluorescent protein and diphtheria toxin receptor. Dendritic cells were found interspersed between renal tubules throughout the tubulointerstitium but not in glomeruli. The functional significance of dendritic cells within their physiological context in cisplatin nephrotoxicity was examined by depleting dendritic cells using diphtheria toxin. Mice depleted of dendritic cells either before or coincident with cisplatin treatment, but not at later stages, exhibited more severe renal dysfunction, kidney tubular injury, neutrophil infiltration and greater mortality than dendritic cell non-depleted mice. Neutrophils and monocytes were abundant in the kidney at later stages of cisplatin nephrotoxicity. In contrast, infiltration of inflammatory dendritic cells was insignificant after cisplatin treatment. Through the use of bone marrow chimeric mice, we also confirmed that the exacerbated renal injury was mediated through the effect of diphtheria toxin on dendritic cells. Using mixed bone marrow chimeric mice, we showed that the worsening of cisplatin nephrotoxicity in dendritic cell-depleted mice occured independent of diphtheria toxin-mediated death of dendritic cells. Analysis of markers on renal dendritic cells after cisplatin treatment showed almost steady-state levels of expression of antigen presentation (MHC class I and MHC class II) and costimulatory molecules (CD40, CD80 and CD86), and an increase in expression of IL-10 and ICOS-L. Further investigation using mixed bone marrow chimeric mice lacking dendritic cell-derived IL-10 showed a moderate level of attenuation of kidney injury by dendritic cell-produced IL-10. These data demonstrate that dendritic cells protect mice from cisplatin nephrotoxicity. Advisors/Committee Members: Judith S Bond, Dissertation Advisor/Co-Advisor, Chair%22%29&pagesize-30">Judith S Bond, Committee Chair/Co-Chair, Chair%22%29&pagesize-30">W. Brian Reeves, Committee Chair/Co-Chair, Cara Lynne Schengrund, Committee Member, Sergei A Grigoryev, Committee Member, Christopher Charles Norbury, Committee Member, Robert Harold Bonneau, Committee Member.

Subjects/Keywords: dendritic cells; acute kidney injury; IL-10

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Tadagavadi, R. K. (2009). Dendritic cells and IL-10 in nephrotoxic acute kidney injury . (Thesis). Penn State University. Retrieved from https://submit-etda.libraries.psu.edu/catalog/10292

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Tadagavadi, Raghu Kempegowda. “Dendritic cells and IL-10 in nephrotoxic acute kidney injury .” 2009. Thesis, Penn State University. Accessed March 03, 2021. https://submit-etda.libraries.psu.edu/catalog/10292.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Tadagavadi, Raghu Kempegowda. “Dendritic cells and IL-10 in nephrotoxic acute kidney injury .” 2009. Web. 03 Mar 2021.

Vancouver:

Tadagavadi RK. Dendritic cells and IL-10 in nephrotoxic acute kidney injury . [Internet] [Thesis]. Penn State University; 2009. [cited 2021 Mar 03]. Available from: https://submit-etda.libraries.psu.edu/catalog/10292.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Tadagavadi RK. Dendritic cells and IL-10 in nephrotoxic acute kidney injury . [Thesis]. Penn State University; 2009. Available from: https://submit-etda.libraries.psu.edu/catalog/10292

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

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