scispace - formally typeset
Search or ask a question
Journal ArticleDOI

Meprins, membrane-bound and secreted astacin metalloproteinases.

TL;DR: The in vivo substrates of meprins are unknown, but the abundant expression of these proteinases in the epithelial cells of the intestine, kidney and skin provide clues to their functions.
About: This article is published in Molecular Aspects of Medicine.The article was published on 2008-10-01 and is currently open access. It has received 178 citations till now. The article focuses on the topics: MATH domain & Astacin.
Citations
More filters
Journal ArticleDOI
TL;DR: Although the colon mucus organization of GF mice was similar to that of conventionally raised (Convr) mice, the GF inner mucus layer was penetrable to bacteria-sized beads, indicating that studies of mature microbe-mucus interactions should be conducted weeks after colonization.

341 citations


Cites background from "Meprins, membrane-bound and secrete..."

  • ...Meprin b is made as an inactive proenzyme and requires proteolytic cleavage for activation (Sterchi et al., 2008)....

    [...]

Journal ArticleDOI
TL;DR: An extensive review of the different MMPs structural and functional features is integrated with their pathological role in several types of diseases, spanning from cancer to cardiovascular diseases and to neurodegeneration.

225 citations


Cites background from "Meprins, membrane-bound and secrete..."

  • ...In humans, there are six astacin genes, including two meprins, three bone morphogenetic protein1 (BMP1)/Tolloid like (TLD) proteases and one ovastacin (Sterchi et al., 2008) (Table 1)....

    [...]

  • ...Astacins family includes several hundred protein detected in species ranging from hydra to humans (for a review see Ge and Greenspan, 2006; Hopkins et al., 2007; Sterchi et al., 2008)....

    [...]

  • ...Meprin subunits a and b cleave a variety of biologically active peptides; in particular, we want to point out gastrin and cholecystokin on one side (which are substrates for meprin b) and substance P and many cytokines on the other side (which are substrates for meprin a, see Sterchi et al., 2008)....

    [...]

Journal ArticleDOI
TL;DR: Seven metzincins families are subdivided into families, and seven such families have been analyzed at the structural level: the astacins, ADAMs/adamalysins/reprolysins, serralysins, matrix metalloproteinases, snapalysins, leishmanolysins, and pappalysins.

214 citations

Journal ArticleDOI
TL;DR: Genetic, biochemical, and histological analyses of this mutant and a comparison to a second, similar locus reveal that Bmp1a is critically required for mature-collagen generation, downstream of osteoblast maturation, in bone.
Abstract: Bone morphogenetic protein 1 (BMP1) is an astacin metalloprotease with important cellular functions and diverse substrates, including extracellular-matrix proteins and antagonists of some TGFβ superfamily members. Combining whole-exome sequencing and filtering for homozygous stretches of identified variants, we found a homozygous causative BMP1 mutation, c.34G>C, in a consanguineous family affected by increased bone mineral density and multiple recurrent fractures. The mutation is located within the BMP1 signal peptide and leads to impaired secretion and an alteration in posttranslational modification. We also characterize a zebrafish bone mutant harboring lesions in bmp1a, demonstrating conservation of BMP1 function in osteogenesis across species. Genetic, biochemical, and histological analyses of this mutant and a comparison to a second, similar locus reveal that Bmp1a is critically required for mature-collagen generation, downstream of osteoblast maturation, in bone. We thus define the molecular and cellular bases of BMP1-dependent osteogenesis and show the importance of this protein for bone formation and stability.

192 citations

Journal ArticleDOI
TL;DR: The indication from cohort studies that there is an association between oxLDL and cardiovascular (CV) events seems to point toward a role for ox LDL in atherosclerotic plaque progress and disruption, but randomized clinical trials using antioxidants have demonstrated benefits only in high-risk patients, suggesting that additional proofs are still needed to better define the involvement of each type of modified LDL in the development of atherosclerosis.

190 citations

References
More filters
Journal ArticleDOI
16 Dec 1988-Science
TL;DR: Human complementary DNA clones corresponding to three polypeptides present in this BMP preparation have been isolated, and expression of the recombinant human proteins have been obtained, and each appears to be independently capable of inducing the formation of cartilage in vivo.
Abstract: Protein extracts derived from bone can initiate the process that begins with cartilage formation and ends in de novo bone formation. The critical components of this extract, termed bone morphogenetic protein (BMP), that direct cartilage and bone formation as well as the constitutive elements supplied by the animal during this process have long remained unclear. Amino acid sequence has been derived from a highly purified preparation of BMP from bovine bone. Now, human complementary DNA clones corresponding to three polypeptides present in this BMP preparation have been isolated, and expression of the recombinant human proteins have been obtained. Each of the three (BMP-1, BMP-2A, and BMP-3) appears to be independently capable of inducing the formation of cartilage in vivo. Two of the encoded proteins (BMP-2A and BMP-3) are new members of the TGF-beta supergene family, while the third, BMP-1, appears to be a novel regulatory molecule.

3,916 citations

Book
01 Jan 1998
TL;DR: In this paper, Serine Peptidases with a Ser/Lys Catalytic Dyad (SC) are described, as well as their relation to the Nodavirus Coat Protein.
Abstract: (Abbreviated Contents Including Section Headings:) Serine Peptidases. Serine Peptidases and Their Clans. Family S1 of Trypsin (Clan SA). Tissue Kallikrein and Its Relatives. Other Families of Clan SA. Clan SB Containing the Subtilisin Family. Clan SC Containing Peptidases with the Alpha/Beta Hydrolase Fold. Clan SE Containing Serine-Type D-Ala-D-Ala Peptidases. Clan SF Containing Peptidases with a Ser/Lys Catalytic Dyad. Clan SH Containing Herpesvirus Assemblins. Clan TA Containing N-Terminal Nucleophile Peptidases. Other Families of Serine Peptidases. Unsequenced Serine Peptidases. Cysteine Peptidases. Cysteine Peptidases and Their Clans. Clan CA Containing Papain and Its Relatives. Clan CC Containing Viral 'Papain Like' Cysteine Endopeptidases. Clan CB Containing the Nodavirus Coat Protein. Other Families of Aspartic Endopeptidases. Metallopeptidases. Metallopeptidases and Their Clans. Clan MA Containing Thermolysin and Its Relatives. Family M1 of Membrane Alanyl Aminopeptidase. Other Families of Clan MA. Family M3 of Thimet Oligopeptidase. Clan MB Containing 'Metzincins' (Clan MB). Family M10 of Interstitial Collagenase (Clan MB). Family M12 of Astacin (Clan MB). Introduction to the Reprolysins (Family M12). Clan MC Containing the Metallocarboxypeptidases. Clan MD Containing Zinc D-Ala-D-Ala-Carboxypeptidase. Clan ME Containing Pitrilysin and Its Relatives. Clan MF Containing Co-Catalytic Leucyl Amino-Peptidases. Clan MG Containing the Methionyl Aminopeptidase Family. Clan MH Containing Varied Co-Catalytic Metallopeptidases. Other Families of Metallopeptidases. Metallopeptidases of Unknown Sequence. Unclassified Peptidases. Peptidases of Unknown Catalytic Type. Subject Index.

2,315 citations

01 Jan 1998
TL;DR: (Abbreviated Contents Including Section Headings:)
Abstract: (Abbreviated Contents Including Section Headings:) Serine Peptidases. Serine Peptidases and Their Clans. Family S1 of Trypsin (Clan SA). Tissue Kallikrein and Its Relatives. Other Families of Clan SA. Clan SB Containing the Subtilisin Family. Clan SC Containing Peptidases with the Alpha/Beta Hydrolase Fold. Clan SE Containing Serine-Type D-Ala-D-Ala Peptidases. Clan SF Containing Peptidases with a Ser/Lys Catalytic Dyad. Clan SH Containing Herpesvirus Assemblins. Clan TA Containing N-Terminal Nucleophile Peptidases. Other Families of Serine Peptidases. Unsequenced Serine Peptidases. Cysteine Peptidases. Cysteine Peptidases and Their Clans. Clan CA Containing Papain and Its Relatives. Clan CC Containing Viral 'Papain Like' Cysteine Endopeptidases. Clan CB Containing the Nodavirus Coat Protein. Other Families of Aspartic Endopeptidases. Metallopeptidases. Metallopeptidases and Their Clans. Clan MA Containing Thermolysin and Its Relatives. Family M1 of Membrane Alanyl Aminopeptidase. Other Families of Clan MA. Family M3 of Thimet Oligopeptidase. Clan MB Containing 'Metzincins' (Clan MB). Family M10 of Interstitial Collagenase (Clan MB). Family M12 of Astacin (Clan MB). Introduction to the Reprolysins (Family M12). Clan MC Containing the Metallocarboxypeptidases. Clan MD Containing Zinc D-Ala-D-Ala-Carboxypeptidase. Clan ME Containing Pitrilysin and Its Relatives. Clan MF Containing Co-Catalytic Leucyl Amino-Peptidases. Clan MG Containing the Methionyl Aminopeptidase Family. Clan MH Containing Varied Co-Catalytic Metallopeptidases. Other Families of Metallopeptidases. Metallopeptidases of Unknown Sequence. Unclassified Peptidases. Peptidases of Unknown Catalytic Type. Subject Index.

1,969 citations

Journal ArticleDOI
TL;DR: Fibronectin mediates a wide variety of cellular interactions with the extracellular matrix (ECM) and plays important roles in cell adhesion, migration, growth and differentiation.
Abstract: Fibronectin (FN) mediates a wide variety of cellular interactions with the extracellular matrix (ECM) and plays important roles in cell adhesion, migration, growth and differentiation ( [Mosher, 1989][1]; [Carsons, 1989][2]; [Hynes, 1990][3]; [Yamada and Clark, 1996][4]). FN is widely expressed by

1,927 citations


"Meprins, membrane-bound and secrete..." refers background in this paper

  • ...…M anuscript N IH -PA Author M anuscript N IH -PA Author M anuscript G1 domain and in the linker between the G1 and G2 domains, and fibronectin is cut within the proteolytically vulnerable linker regions between fibronectin type III repeats 1 and 2, 3 and 4, and 5 and 6 (Pankov and Yamada 2002)....

    [...]