TY - JOUR
T1 - Distribution patterns of the anti-angiogenic protein ADAMTS-1 during rat development
AU - Günther, Willy
AU - Skaftnesmo, Kai Ove
AU - Arnold, Hans
AU - Bjerkvig, Rolf
AU - Terzis, A. Jorge A.
N1 - Funding Information:
This study was supported by The Norwegian Cancer Society, the Norwegian Research Council, the University of Lübeck, University of Bergen and Centre de Recherche Public Santé, Luxembourg.
PY - 2005/7/1
Y1 - 2005/7/1
N2 - 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 62 kDa 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.
AB - 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 62 kDa 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.
KW - Adamts-1
KW - Development
KW - Meth-1
KW - Rat
UR - http://www.scopus.com/inward/record.url?scp=20444402255&partnerID=8YFLogxK
U2 - 10.1016/j.acthis.2004.07.009
DO - 10.1016/j.acthis.2004.07.009
M3 - Article
C2 - 15878613
AN - SCOPUS:20444402255
SN - 0065-1281
VL - 107
SP - 121
EP - 131
JO - Acta Histochemica
JF - Acta Histochemica
IS - 2
ER -