Mesangial cell-matrix interactions: modulation of matrix expression in mesangial cells by extracellular matrices. 1995

M Sakatsume, and A Saito, and T Takeda, and H Yamazaki, and I Narita, and S Nishi, and Y Nakagawa, and M Arakawa
Department of Medicine (II), Niigata University School of Medicine, Japan.

Aberrant extracellular matrices (ECMs) observed in mesangial areas during the progression of glomerulonephropathy could be produced by mesangial cells (MCs), interacting with altered ECM components, under the influence of various mediators. We studied the interaction between MCs and ECMs, especially focusing on matrix expression of MCs in contact with ECMs. We analyzed mRNA expression and protein synthesis of ECM components by cultured rat MCs which were plated on different types of ECMs, basement membrane-type matrix (BMM), type IV collagen and type I collagen. The level of mRNA for ECM components (alpha 1 type I collagen, alpha 1 type IV collagen, fibronectin and laminin B2) increased in MCs on the two types of collagen compared with BMM. The relative increase of alpha 1 type I collagen mRNA expression in MCs on type I collagen was greater than that of alpha 1 type IV collagen expression. At the protein level, type I collagen production by MCs on coated type I collagen showed a 2.2-fold increase relative to that on BMM. MCs on type IV collagen produced it at an intermediate level. The phenomena were not associated with differences of proliferative activity, but were accompanied by minor morphological differences. These results indicate that ECMs can modulate the phenotype of MCs in terms of matrix expression and suggest that MC-matrix interaction may in part contribute to abnormal ECM accumulation in diseased glomeruli.

UI MeSH Term Description Entries
D007797 Laminin Large, noncollagenous glycoprotein with antigenic properties. It is localized in the basement membrane lamina lucida and functions to bind epithelial cells to the basement membrane. Evidence suggests that the protein plays a role in tumor invasion. Merosin,Glycoprotein GP-2,Laminin M,Laminin M Chain,Chain, Laminin M,Glycoprotein GP 2,M Chain, Laminin
D008297 Male Males
D002455 Cell Division The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION. M Phase,Cell Division Phase,Cell Divisions,Division Phase, Cell,Division, Cell,Divisions, Cell,M Phases,Phase, Cell Division,Phase, M,Phases, M
D003094 Collagen A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH). Avicon,Avitene,Collagen Felt,Collagen Fleece,Collagenfleece,Collastat,Dermodress,Microfibril Collagen Hemostat,Pangen,Zyderm,alpha-Collagen,Collagen Hemostat, Microfibril,alpha Collagen
D005109 Extracellular Matrix A meshwork-like substance found within the extracellular space and in association with the basement membrane of the cell surface. It promotes cellular proliferation and provides a supporting structure to which cells or cell lysates in culture dishes adhere. Matrix, Extracellular,Extracellular Matrices,Matrices, Extracellular
D005353 Fibronectins Glycoproteins found on the surfaces of cells, particularly in fibrillar structures. The proteins are lost or reduced when these cells undergo viral or chemical transformation. They are highly susceptible to proteolysis and are substrates for activated blood coagulation factor VIII. The forms present in plasma are called cold-insoluble globulins. Cold-Insoluble Globulins,LETS Proteins,Fibronectin,Opsonic Glycoprotein,Opsonic alpha(2)SB Glycoprotein,alpha 2-Surface Binding Glycoprotein,Cold Insoluble Globulins,Globulins, Cold-Insoluble,Glycoprotein, Opsonic,Proteins, LETS,alpha 2 Surface Binding Glycoprotein
D005920 Glomerular Mesangium The thin membranous structure supporting the adjoining glomerular capillaries. It is composed of GLOMERULAR MESANGIAL CELLS and their EXTRACELLULAR MATRIX. Mesangium, Glomerular,Mesangial Extracellular Matrix,Extracellular Matrices, Mesangial,Extracellular Matrix, Mesangial,Glomerular Mesangiums,Matrices, Mesangial Extracellular,Matrix, Mesangial Extracellular,Mesangial Extracellular Matrices,Mesangiums, Glomerular
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001485 Basement Membrane A darkly stained mat-like EXTRACELLULAR MATRIX (ECM) that separates cell layers, such as EPITHELIUM from ENDOTHELIUM or a layer of CONNECTIVE TISSUE. The ECM layer that supports an overlying EPITHELIUM or ENDOTHELIUM is called basal lamina. Basement membrane (BM) can be formed by the fusion of either two adjacent basal laminae or a basal lamina with an adjacent reticular lamina of connective tissue. BM, composed mainly of TYPE IV COLLAGEN; glycoprotein LAMININ; and PROTEOGLYCAN, provides barriers as well as channels between interacting cell layers. Basal Lamina,Basement Lamina,Lamina Densa,Lamina Lucida,Lamina Reticularis,Basement Membranes,Densas, Lamina,Lamina, Basal,Lamina, Basement,Lucida, Lamina,Membrane, Basement,Membranes, Basement,Reticularis, Lamina
D012333 RNA, Messenger RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm. Messenger RNA,Messenger RNA, Polyadenylated,Poly(A) Tail,Poly(A)+ RNA,Poly(A)+ mRNA,RNA, Messenger, Polyadenylated,RNA, Polyadenylated,mRNA,mRNA, Non-Polyadenylated,mRNA, Polyadenylated,Non-Polyadenylated mRNA,Poly(A) RNA,Polyadenylated mRNA,Non Polyadenylated mRNA,Polyadenylated Messenger RNA,Polyadenylated RNA,RNA, Polyadenylated Messenger,mRNA, Non Polyadenylated

Related Publications

M Sakatsume, and A Saito, and T Takeda, and H Yamazaki, and I Narita, and S Nishi, and Y Nakagawa, and M Arakawa
May 2002, Biochimica et biophysica acta,
M Sakatsume, and A Saito, and T Takeda, and H Yamazaki, and I Narita, and S Nishi, and Y Nakagawa, and M Arakawa
January 1994, Srpski arhiv za celokupno lekarstvo,
M Sakatsume, and A Saito, and T Takeda, and H Yamazaki, and I Narita, and S Nishi, and Y Nakagawa, and M Arakawa
October 1998, Annals of the New York Academy of Sciences,
M Sakatsume, and A Saito, and T Takeda, and H Yamazaki, and I Narita, and S Nishi, and Y Nakagawa, and M Arakawa
December 1988, The American journal of pathology,
M Sakatsume, and A Saito, and T Takeda, and H Yamazaki, and I Narita, and S Nishi, and Y Nakagawa, and M Arakawa
April 1992, Journal of the American Society of Nephrology : JASN,
M Sakatsume, and A Saito, and T Takeda, and H Yamazaki, and I Narita, and S Nishi, and Y Nakagawa, and M Arakawa
June 1991, Experimental and molecular pathology,
M Sakatsume, and A Saito, and T Takeda, and H Yamazaki, and I Narita, and S Nishi, and Y Nakagawa, and M Arakawa
April 1992, Experimental and molecular pathology,
M Sakatsume, and A Saito, and T Takeda, and H Yamazaki, and I Narita, and S Nishi, and Y Nakagawa, and M Arakawa
March 1993, Journal of periodontal research,
M Sakatsume, and A Saito, and T Takeda, and H Yamazaki, and I Narita, and S Nishi, and Y Nakagawa, and M Arakawa
January 2015, International journal of clinical and experimental medicine,
M Sakatsume, and A Saito, and T Takeda, and H Yamazaki, and I Narita, and S Nishi, and Y Nakagawa, and M Arakawa
April 1989, The American journal of pathology,
Copied contents to your clipboard!