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J. Biol. Chem., Vol. 276, Issue 21, 17932-17940, May 25, 2001
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From the We have identified and cloned a human fetal lung
cDNA encoding a new protein of the ADAM-TS family (a
disintegrin and metalloproteinase domain, with thrombospondin type-1 modules)
that has been called ADAM-TS12. This protein exhibits a domain
organization similar to the remaining family members including a
propeptide and metalloproteinase-like, disintegrin-like, and
cysteine-rich domains. However, the number and organization of the TS
repeats is unique with respect to other human ADAM-TSs. A total of
eight TS-1 repeats arranged in three groups are present in this novel
ADAM-TS. Analysis of intracellular processing of ADAM-TS12 revealed
that it is synthesized as a precursor molecule that is first activated
by cleavage of the prodomain in a furin-mediated process and
subsequently processed into two fragments of different size: a 120-kDa
N-terminal proteolytically active fragment containing the
metalloproteinase and disintegrin domains, and a 83-kDa C-terminal
fragment containing most of the TS-1 repeats. Somatic cell hybrid and
radiation hybrid mapping experiments showed that the human ADAM-TS12
gene maps to 5q35, a location that differs from all ADAM genes mapped
to date. Northern blot analysis of RNAs from human adult and fetal
tissues demonstrated that ADAM-TS12 transcripts are only detected at
significant levels in fetal lung but not in any other analyzed tissues.
In addition, ADAM-TS12 transcripts were detected in gastric carcinomas
and in tumor cell lines from diverse sources, being induced by
transforming growth factor- The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ250725.
Identification, Characterization, and Intracellular Processing of
ADAM-TS12, a Novel Human Disintegrin with a Complex Structural
Organization Involving Multiple Thrombospondin-1 Repeats*
§,,
Departamento de Bioquímica y
Biología Molecular, Facultad de Medicina, Instituto
Universitario de Oncología, Universidad de Oviedo, 33006 Oviedo
and ¶ Servicio de Anatomía Patológica, Hospital
Clínico-IDIBAPS, 08036 Barcelona, Spain
in KMST human fibroblasts. These
data suggest that ADAM-TS12 may play roles in pulmonary cells during
fetal development or in tumor processes through its proteolytic
activity or as a molecule potentially involved in regulation of cell adhesion.
*
This work was supported by Comisión Interministerial
de Ciencia y Tecnología-Spain Grant SAF97-0258 and Plan Fondos
Europeos para el Desarrollo Regional Grant 1FD97-0214. The Instituto
Universitario de Oncología is supported by Obra Social
Cajastur-Asturias.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Departamento de
Bioquímica y Biología Molecular, Facultad de Medicina,
Universidad de Oviedo, 33006 Oviedo, Spain. Tel.: 34-985-104201;
Fax: 34-985-103564; E-mail: CLO@correo.uniovi.es.
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