Literature DB >> 10506182

MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes.

C M Roberts1, P H Tani, L C Bridges, Z Laszik, R D Bowditch.   

Abstract

The metalloprotease disintegrin cysteine-rich (MDC) proteins are a recently identified family of transmembrane proteins that function in proteolytic processing of cell surface molecules and in cell adhesion. Since lymphocytes must interact with a constantly changing environment, we hypothesized that lymphocytes would express unique MDC proteins. To identify MDC proteins expressed in human lymph node, a polymerase chain reaction-based strategy combined with degenerate oligonucleotide primers was employed. We report here the identification of MDC-L (ADAM 23), a novel member of the MDC protein family. The results obtained from cDNA cloning and Northern blot analysis of mRNA isolated from various lymphoid tissues indicate that a 2.8-kilobase mRNA encoding a transmembrane form, MDC-Lm, and a 2.2-kilobase mRNA encoding a secreted form, MDC-Ls, are expressed in a tissue-specific manner. MDC-L mRNA was shown to be predominantly expressed in secondary lymphoid tissues, such as lymph node, spleen, small intestine, stomach, colon, appendix, and trachea. Furthermore, immunohistochemical staining with an anti-MDC-L antibody demonstrated that cells with typical lymphocyte morphology are responsible for expression of the MDC-L antigen in these lymphoid tissues. MDC-Lm was found to be expressed on the surface of human peripheral blood lymphocytes and transformed B- and T-lymphocyte cell lines as an 87-kDa protein. Thus, we have identified a novel lymphocyte-expressed MDC protein family member.

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Year:  1999        PMID: 10506182     DOI: 10.1074/jbc.274.41.29251

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  12 in total

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Review 2.  Metalloproteinases and their inhibitors: regulators of wound healing.

Authors:  Sean E Gill; William C Parks
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3.  Stall encodes an ADAMTS metalloprotease and interacts genetically with Delta in Drosophila ovarian follicle formation.

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4.  Domain integration of ADAM family proteins: Emerging themes from structural studies.

Authors:  Tom Cm Seegar; Stephen C Blacklow
Journal:  Exp Biol Med (Maywood)       Date:  2019-07-23

5.  9-cis-retinoic acid promotes cell adhesion through integrin dependent and independent mechanisms across immune lineages.

Authors:  Jarrett T Whelan; Jianming Chen; Jabin Miller; Rebekah L Morrow; Joshuah D Lingo; Kaitlin Merrell; Saame Raza Shaikh; Lance C Bridges
Journal:  J Nutr Biochem       Date:  2012-08-25       Impact factor: 6.048

6.  Conservation and divergence of ADAM family proteins in the Xenopus genome.

Authors:  Shuo Wei; Charles A Whittaker; Guofeng Xu; Lance C Bridges; Anoop Shah; Judith M White; Douglas W Desimone
Journal:  BMC Evol Biol       Date:  2010-07-14       Impact factor: 3.260

7.  Maternal age effects on myometrial expression of contractile proteins, uterine gene expression, and contractile activity during labor in the rat.

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8.  Alternative mRNA splicing generates two distinct ADAM12 prodomain variants.

Authors:  Sara Duhachek-Muggy; Hui Li; Yue Qi; Anna Zolkiewska
Journal:  PLoS One       Date:  2013-10-07       Impact factor: 3.240

9.  Urinary concentrations of ADAM 12 from breast cancer patients pre- and post-surgery vs. cancer-free controls: a clinical study for biomarker validation.

Authors:  Erin K Nyren-Erickson; Michael Bouton; Mihir Raval; Jessica Totzauer; Sanku Mallik; Neville Alberto
Journal:  J Negat Results Biomed       Date:  2014-04-01

Review 10.  ADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural Overview.

Authors:  Soichi Takeda
Journal:  Toxins (Basel)       Date:  2016-05-17       Impact factor: 4.546

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