Literature DB >> 7545202

Matrix metalloproteinases in blood vessel development in human fetal skin and in cutaneous tumors.

T V Karelina1, G I Goldberg, A Z Eisen.   

Abstract

In vitro angiogenesis models suggest that new blood vessel formation requires the induction and secretion by endothelial cells of matrix metalloproteinases. These enzymes assist in the controlled proteolytic degradation of the surrounding extracellular matrix during blood vessel formation. The results of in vitro studies cannot be extrapolated directly to the process of in vivo angiogenesis because the type of matrix employed and the repertoire of enzymes secreted by cells in vivo differ dramatically from in vivo conditions. To investigate the in vivo role of matrix metalloproteinases in blood vessel development, we looked for the presence of these proteinases in endothelial cells involved in fetal angiogenesis and in neovascularization of certain invasive skin tumors using immunofluorescent staining. In fetal tissue, interstitial collagenase was present in both early microvessels developing from undifferentiated mesoderm and in microvessels involved in elongation and sprout formation from preexisting blood vessels. In aggressive skin tumors, i.e., morpheaform and recurrent basal cell carcinomas and squamous cell carcinomas, there was a marked increase in the number of collagenase-containing blood vessels, often extending into the tumor nests. Immunofluorescent staining failed to detect stromelysin, matrilysin, or gelatinase A and B (72- and 92-kDa type IV collagenases, respectively) in fetal or tumor blood vessels. These findings are consistent with the hypothesis that proteolytic degradation of the extracellular matrix is required for the formation of new blood vessels. Interstitial collagenase appears to play an important role in this process.

Entities:  

Mesh:

Substances:

Year:  1995        PMID: 7545202     DOI: 10.1111/1523-1747.ep12321097

Source DB:  PubMed          Journal:  J Invest Dermatol        ISSN: 0022-202X            Impact factor:   8.551


  9 in total

1.  Distribution of matrix metalloproteinases and their inhibitor, TIMP-1, in developing human osteophytic bone.

Authors:  S Bord; A Horner; R M Hembry; J J Reynolds; J E Compston
Journal:  J Anat       Date:  1997-07       Impact factor: 2.610

2.  Activation of gelatinase-tissue-inhibitors-of-metalloproteinase complexes by matrilysin.

Authors:  D C von Bredow; A E Cress; E W Howard; G T Bowden; R B Nagle
Journal:  Biochem J       Date:  1998-05-01       Impact factor: 3.857

3.  MMP-9/gelatinase B is a key regulator of growth plate angiogenesis and apoptosis of hypertrophic chondrocytes.

Authors:  T H Vu; J M Shipley; G Bergers; J E Berger; J A Helms; D Hanahan; S D Shapiro; R M Senior; Z Werb
Journal:  Cell       Date:  1998-05-01       Impact factor: 41.582

4.  Temporal expression of the matrix metalloproteinase MMP-2 correlates with fibronectin immunoreactivity during the development of the vascular system in the chick embryo chorioallantoic membrane.

Authors:  D Ribatti; B Nico; A Vacca; M Iurlaro; L Roncali
Journal:  J Anat       Date:  1999-07       Impact factor: 2.610

Review 5.  Breast cancer in the clinic: treatments past, treatments future.

Authors:  G W Sledge
Journal:  J Mammary Gland Biol Neoplasia       Date:  2001-10       Impact factor: 2.673

Review 6.  The role of matrix metalloproteinases in tumor angiogenesis and tumor metastasis.

Authors:  A John; G Tuszynski
Journal:  Pathol Oncol Res       Date:  2001       Impact factor: 3.201

7.  Matrix metalloproteinase-1 promotes prostate tumor growth and metastasis.

Authors:  Sai Murali Krishna Pulukuri; Jasti S Rao
Journal:  Int J Oncol       Date:  2008-04       Impact factor: 5.650

Review 8.  Craniofacial and Long Bone Development in the Context of Distraction Osteogenesis.

Authors:  Harsh N Shah; Ruth E Jones; Mimi R Borrelli; Kiana Robertson; Ankit Salhotra; Derrick C Wan; Michael T Longaker
Journal:  Plast Reconstr Surg       Date:  2021-01-01       Impact factor: 5.169

9.  Regulation of monocyte MMP-9 production by TNF-alpha and a tumour-derived soluble factor (MMPSF).

Authors:  T M Leber; F R Balkwill
Journal:  Br J Cancer       Date:  1998-09       Impact factor: 7.640

  9 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.