Distribution patterns of the anti-angiogenic protein ADAMTS-1 during rat development

被引:23
作者
Günther, W
Skaftnesmo, KO
Arnold, H
Bjerkvig, R
Terzis, AJA [1 ]
机构
[1] Univ Bergen, Sect Anat & Cell Biol, Dept Biomed, NorLux Neurooncol, N-5009 Bergen, Norway
[2] Med Univ Lubeck, Dept Neurosurg, D-23538 Lubeck, Germany
[3] Ctr Rech Publ Sante, NorLux Neurooncol, Luxembourg, Luxembourg
关键词
Meth-1; Adamts-1; rat; development;
D O I
10.1016/j.acthis.2004.07.009
中图分类号
Q2 [细胞生物学];
学科分类号
071009 [细胞生物学]; 090102 [作物遗传育种];
摘要
A disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS-1) belongs to the large ADAM family of proteins. ADAMTS-1 contains a metalloproteinase domain, a disintegrin domain and three thrombospondin-like repeats but unlike ADAMs lacks a transmembrane domain. For the elucidation of the biological functions of ADAMTS-1, we raised new antibodies against ADAMTS-1. We show an accumulation of ADAMTS-1 protein at the basal lamina of rat embryonal epithelia of intestines, nasal cavity, choroid plexus, skin and in intracellular storage vesicles of epithelial cells. ADAMTS-1 protein seems to play a role in the development of the neuronal system, adipose tissue, muscle, heart, liver and adrenal glands. At the time of birth its presence is reduced in most organs. However, in the developing bone as well as in the skin, labelling increased towards late embryonal development. Immunoblots revealed a strong presence of a 62kDa ADAMTS-1 fragment in kidneys, adrenal glands, lungs, intestines and heart. ADAMTS-1 was also present in the corresponding adult rat organs, but in more restricted distribution patterns. It was typically found in principal cells of collecting ducts, of the renal medulla, in ependymal cells of the ventricles and in some neurons. The results were confirmed by real-time PCR, The specific distribution pattern of ADAMTS-1 in a variety of organs during embryogenesis suggests a role of the molecule in tissue remodelling, vasculogenesis and angiogenesis. (c) 2005 Published by Elsevier GmbH.
引用
收藏
页码:121 / 131
页数:11
相关论文
共 27 条
[1]
Metalloprotease-disintegrins: Links to cell adhesion and cleavage of TNF alpha and notch [J].
Blobel, CP .
CELL, 1997, 90 (04) :589-592
[2]
Interactions between tumour cells and stromal cells and proteolytic modification of the extracellular matrix by metalloproteinases in cancer [J].
DeClerck, YA .
EUROPEAN JOURNAL OF CANCER, 2000, 36 (10) :1258-1268
[3]
Cloning of the rat ADAMTS-1 gene and its down regulation in endothelial cells in cirrhotic rats [J].
Diamantis, I ;
Lüthi, M ;
Hösli, M ;
Reichen, J .
LIVER, 2000, 20 (02) :165-172
[4]
Ovarian expression of a disintegrin and metalloproteinase with thrombospondin motifs during ovulation in the gonadotropin-primed immature rat [J].
Espey, LL ;
Yoshioka, S ;
Russell, DL ;
Robker, RL ;
Fujii, S ;
Richards, JS .
BIOLOGY OF REPRODUCTION, 2000, 62 (04) :1090-1095
[5]
COLOR MODIFICATION OF DIAMINOBENZIDINE (DAB) PRECIPITATION BY METALLIC-IONS AND ITS APPLICATION FOR DOUBLE IMMUNOHISTOCHEMISTRY [J].
HSU, SM ;
SOBAN, E .
JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY, 1982, 30 (10) :1079-1082
[6]
ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases - General features and genomic distribution of the ADAM-TS family [J].
Hurskainen, TL ;
Hirohata, S ;
Seldin, MF ;
Apte, SS .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (36) :25555-25563
[7]
The new kids on the block: ADAMTSs, potentially multifunctional metalloproteinases of the ADAM family [J].
Kaushal, GP ;
Shah, SV .
JOURNAL OF CLINICAL INVESTIGATION, 2000, 105 (10) :1335-1337
[8]
Shedding light on sheddases: role in growth and development [J].
Kheradmand, F ;
Werb, Z .
BIOESSAYS, 2002, 24 (01) :8-12
[9]
Kuno K, 1997, J BIOL CHEM, V272, P556, DOI 10.1074/jbc.272.1.556
[10]
ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region [J].
Kuno, K ;
Matsushima, K .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (22) :13912-13917