Publication: Expression, function and clinical relevance of
MIA (Melanoma Inhibitory Activity)
Authors
Bosserhoff, A.K. ; Buettner, R.
item.page.secondaryauthor
item.page.director
Publisher
Murcia : F. Hernández
publication.page.editor
publication.page.department
DOI
item.page.type
info:eu-repo/semantics/article
Description
Abstract
Despite its ambiguous name the protein
melanoma-inhibitory-activity (MIA) was identified as a
key molecule involved in progression and metastasis of
malignant melanomas. Therefore, in this review we
intend to update the current knowledge on expression
patterns, transcriptional regulation, function and clinical
relevance of MIA. Furthermore, we will cover the
recently discovered MIA homologous proteins
OTOR/MIAL, MIA 2 and TANGO.
In order to identify autocrine growth-regulatory
factors secreted by melanoma cells, MIA was purified
and cloned. Subsequent analyses of non-neoplastic
tissues revealed specific MIA expression patterns in
cartilage. In neoplastic tissues MIA expression was
detected in malignant melanomas, in chondrosarcomas
and less frequently in a variety of diff e r e n t
adenocarcinomas including breast and colon cancers.
For melanoma cells and chondrocytes it was shown that
regulation of expression pattern was controlled on the
level of mRNA transcription by defined transcription
factors.
Evidence obtained from in vitro and in vivo
experiments indicated that MIA plays an important
functional role in melanoma metastasis and invasion. A
number of studies from different laboratories evaluated
MIA as a highly specific and sensitive marker, clinically
useful for follow-up and therapy-monitoring of patients
with malignant melanomas. In addition, preliminary data
suggests a further potential application as a surrogate
marker for measuring cartilage damage in rheumatoid
arthritis.
Recently, it has become evident that MIA belongs to
a gene family of four homologous proteins, MIA, OTOR
(FDP, MIAL), MIA 2 and TANGO. Determination of the
three-dimensional structure in solution identified MIA as
the first member of this novel family of secreted,
extracellular proteins adopting an SH3 domain-like fold.
The data suggest specific protein-protein interactions
with components of the extracellular matrix and possibly
publication.page.subject
Citation
item.page.embargo
Ir a Estadísticas
Sin licencia Creative Commons.