+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Cloning of a human gene potentially encoding a novel matrix metalloproteinase having a C-terminal transmembrane domain



Cloning of a human gene potentially encoding a novel matrix metalloproteinase having a C-terminal transmembrane domain



Gene (amsterdam). 155(2): 293-298



Matrix metalloproteinases (MMPs) play key roles in tissue remodeling during physiological and pathological processes by degrading various extracellular matrix (ECM) components. Although nine distinct MMPs have been characterized by cDNA cloning, there are thought to be more corresponding to the complexity of the ECM. MMP genes expressed in human tissues and cell lines were analyzed by the polymerase chain reaction (PCR) using degenerate primers that corresponded to the conserved amino acid (aa) sequences of the MMPs. One isolated complementary DNA (cDNA) fragment had sequence homology to the reported MMPs, but was otherwise unique. A human placenta cDNA library (Clontech) was screened using the fragment as a probe and a 3.4-kb cDNA fragment containing a long open reading frame (potentially encoding 582 aa) was isolated. The putative gene product had a common domain structure and the conserved sequence of a MMP, but it had a unique transmembrane (TM)-like structure at the C terminus. It should, therefore, be an TM protein, whereas all the other reported MMPs are secretory proteins. Thus, the gene is thought to be the first of a new subclass of MMPs whose products are potentially expressed on the cell surface.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 008334488

Download citation: RISBibTeXText

PMID: 7721107

DOI: 10.1016/0378-1119(94)00637-8


Related references

Cloning of a gene encoding a novel matrix metalloproteinase with a transmembrane structure. Clinical & Experimental Metastasis 12(5): 63, 1994

The C-terminal region of membrane type matrix metalloproteinase is a functional transmembrane domain required for pro-gelatinase A activation. Journal of Biological Chemistry 270(2): 801-805, 1995

Molecular cloning of a gene encoding matrix metalloproteinase-like protein from Gnathostoma spinigerum. Parasitology Research 87(9): 751-757, 2001

Backbone NMR assignment of the C-terminal haemopexin-like domain (HPLD) of human matrix metalloproteinase MMP-13. Journal of Biomolecular Nmr 32(4): 337-337, 2005

A transmembrane trap method for efficient cloning of genes encoding proteins possessing transmembrane domain. Biochemical and Biophysical Research Communications 289(5): 1192-1198, 2001

Cloning of a human epididymis-specific mRNA, HE6, encoding a novel member of the seven transmembrane-domain receptor superfamily. Dna & Cell Biology. 16(4): 379-389, 1997

Quantitative analysis of gene expressions of matrix metalloproteinase 2 , tissue inhibitor of metalloproteinase 2 , and membrane type matrix metalloproteinase in human bladder cancers. Journal of Urology 157(4 Suppl. ): 148, 1997

Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors. Journal of Biological Inorganic Chemistry 12(8): 1197-1206, 2007

Molecular cloning of a cDNA encoding a novel human protein with a D-AKPA2 sequence at its carboxyl terminal domain. FASEB Journal 12(8): A1374, 1998

Peptide from the C-terminal domain of tissue inhibitor of matrix metalloproteinases-2 (TIMP-2) inhibits membrane activation of matrix metalloproteinase-2 (MMP-2). Matrix Biology 30(7-8): 404-412, 2011

Cloning of the gene for interstitial collagenase-3 (matrix metalloproteinase-13) from rabbit synovial fibroblasts: differential expression with collagenase-1 (matrix metalloproteinase-1). Biochemical Journal 331: 341-346, 1998

The second zinc atom in the matrix metalloproteinase catalytic domain is absent in the full-length enzymes: A possible role for the C-terminal domain. FEBS Letters 358(2): 189-192, 1995