• shareshare
  • link
  • cite
  • add
auto_awesome_motion View all 2 versions
Publication . Article . 2009

Regulation of Type IV Collagen α Chains of Glomerular Epithelial Cells in Diabetic Conditions

Tae-Sun Ha; Eun-Jeong Hong; Eun-Mi Ahn; Hee-Yul Ahn;
Open Access
Published: 01 Sep 2009 Journal: Journal of Korean Medical Science, volume 24, issue 5, pages 837-843 (issn: 1011-8934, eissn: 1598-6357, Copyright policy )
Publisher: The Korean Academy of Medical Sciences

An early feature of diabetic nephropathy is the alteration of the glomerular basement membrane (GBM), which may result in microalbuminuria, subsequent macroproteinuria, and eventual chronic renal failure. Although type IV collagen is the main component of thickened GBM in diabetic nephropathy, cellular metabolism of each α chains of type IV collagen has not been well studied. To investigate the regulation of α(IV) chains in diabetic conditions, we examined whether glucose and advanced glycosylation endproduct (AGE) regulate the metabolism of each α(IV) chains in the diabetic tissue and glomerular epithelial cells (GEpC). Glomerular collagen α3(IV) and α5(IV) chains protein were higher and more intense in immunofluorescence staining according to diabetic durations compared to controls. In vitro, mainly high glucose and partly AGE usually increased total collagen protein of GEpC by [3H]-proline incorporation assay and each α(IV) chain proteins including α1(IV), α3(IV), and α5(IV) in time-dependent and subchain-specific manners. However, the changes of each α(IV) chains mRNA expression was not well correlated to the those of each chain proteins. The present findings suggest that the metabolism of individual α(IV) chains of GBM is differentially regulated in diabetic conditions and those changes might be induced not only by transcriptional level but also by post-translational modifications.

Subjects by Vocabulary

Microsoft Academic Graph classification: Microalbuminuria medicine.disease medicine Glycosylation chemistry.chemical_compound chemistry Internal medicine medicine.medical_specialty Endocrinology Alpha (ethology) Diabetic nephropathy Glomerular basement membrane medicine.anatomical_structure Biology Metabolism Type IV collagen In vitro


Original Article, Glycosylation End Products, Advanced, Diabetic Nephropathies, Collagen Type IV, Glucose, Podocytes, General Medicine

Related Organizations
30 references, page 1 of 3

Sowers, JR, Epstein, M, Frohlich, ED. Diabetes, hypertension, and cardiovascular disease: an update. Hypertension. 2001; 37: 1053-1059 [PubMed]

Sharma, K, Ziyadeh, FN. Hyperglycemia and diabetic kidney disease. The case for transforming growth factor-beta as a key mediator. Diabetes. 1995; 44: 1139-1146 [OpenAIRE] [PubMed]

Cooper, ME. Pathogenesis, prevention, and treatment of diabetic nephropathy. Lancet. 1998; 352: 213-219 [PubMed]

Ziyadeh, FN, Sharma, K, Ericksen, M, Wolf, G. Stimulation of collagen gene expression and protein synthesis in murine mesangial cells by high glucose is mediated by autocrine activation of transforming growth factor-beta. J Clin Invest. 1994; 93: 536-542 [OpenAIRE] [PubMed]

Hoffman, B, Sharma, K, Zhu, Y, Ziyadeh, FN. Transcriptional activation of transforming growth factor-beta1 in mesangial cell culture by high glucose concentration. Kidney Int. 1998; 54: 1107-1116 [OpenAIRE] [PubMed]

Ziyadeh, FN. The extracellular matrix in diabetic nephropathy. Am J Kidney Dis. 1993; 22: 736-744 [OpenAIRE] [PubMed]

Yurchenco, PD, Smirnov, S, Mathus, T. Analysis of basement membrane self-assembly and cellular interactions with native and recombinant glycoproteins. Methods Cell Biol. 2002; 69: 111-144 [OpenAIRE] [PubMed]

Aumailley, M, Gayraud, B. Structure and biological activity of the extracellular matrix. J Mol Med. 1998; 76: 253-265 [PubMed]

Miner, JH. Renal basement membrane components. Kidney Int. 1999; 56: 2016-2024 [PubMed]

Hostikka, SL, Eddy, RL, Byers, MG, Hoyhtya, M, Shows, TB, Tryggvason, K. Identification of a distinct type IV collagen alpha chain with restricted kidney distribution and assignment of its gene to the locus of X chromosome-linked Alport syndrome. Proc Natl Acad Sci USA. 1990; 87: 1606-1610 [OpenAIRE] [PubMed]

Download fromView all 2 sources