PMID- 8617992
OWN - NLM
STAT- MEDLINE
DCOM- 19960613
LR  - 20191210
IS  - 0022-202X (Print)
IS  - 0022-202X (Linking)
VI  - 106
IP  - 4
DP  - 1996 Apr
TI  - Characterization and subcellular localization of human Pmel 17/silver, a 110-kDa 
      (pre)melanosomal membrane protein associated with 
      5,6,-dihydroxyindole-2-carboxylic acid (DHICA) converting activity.
PG  - 605-10
AB  - Pmel 17 is preferentially expressed in pigment cells in a manner suggestive of 
      involvement in melanin biosynthesis. The gene is identical to the silver (si) 
      pigmentation locus in mice. We now produced a recombinant 
      glutathione-S-transferase-human Pmel 17 infusion protein and raised polyclonal 
      antibodies against it to confirm the ultrastructural location and presumed site 
      of action predicted by the deduced primary structure of Pmel 17/silver, and to 
      authenticate the specificity of the DHICA converting function as inherent to the 
      silver-locus protein. Full-length Pmel 17 cDNA also produced in insect cells in a 
      baculovirus expression vector to ensure that activity did not originate from a 
      co-precipitated protein. Natural hPmel 17 from human melanoma cells has an 
      approximate molecular size of 100 kDa. By immunoperoxidase electron microscopic 
      cytochemistry, the antigen was localized to the limiting membranes of 
      premelanosomes and presumed premelanogenic cytosolic vesicles and, to a minor 
      extent, in the premelanosomal matrix. In an in vitro assay, both the natural and 
      the recombinant Pmel 17 accelerated the conversion of DHICA to melanin. This 
      activity was inhibited by the anti-Pmel 17 polyclonal antibodies, indicating that 
      the acceleration of DHICA conversion by natural protein is genuine and cannot be 
      due to contaminating complexed proteins. We suggest that in situ Pmel 17/silver 
      is a component of a postulated premelanosomal/melanosomal complex of 
      membrane-bound melanogenic oxidoreductive enzymes and cofactors, in analogy to 
      the electron transfer chain in mitochondria.
FAU - Lee, Z H
AU  - Lee ZH
AD  - Department of Microbiology and Immunology, Indiana University School of Medicine, 
      Indianapolis, USA.
FAU - Hou, L
AU  - Hou L
FAU - Moellmann, G
AU  - Moellmann G
FAU - Kuklinska, E
AU  - Kuklinska E
FAU - Antol, K
AU  - Antol K
FAU - Fraser, M
AU  - Fraser M
FAU - Halaban, R
AU  - Halaban R
FAU - Kwon, B S
AU  - Kwon BS
LA  - eng
GR  - AR 39848/AR/NIAMS NIH HHS/United States
GR  - R01 AI22610/AI/NIAID NIH HHS/United States
GR  - R01 AR40248/AR/NIAMS NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Invest Dermatol
JT  - The Journal of investigative dermatology
JID - 0426720
RN  - 0 (Indoles)
RN  - 0 (Melanins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (PMEL protein, human)
RN  - 0 (Pmel protein, mouse)
RN  - 0 (Proteins)
RN  - 0 (gp100 Melanoma Antigen)
RN  - 4790-08-3 (5,6-dihydroxy-2-indolylcarboxylic acid)
RN  - EC 1.- (Oxidoreductases)
RN  - EC 1.14.18.- (TYRP1 protein, human)
RN  - EC 1.14.18.- (tyrosinase-related protein-1)
SB  - IM
MH  - Animals
MH  - Humans
MH  - Indoles/*metabolism
MH  - Melanins/*metabolism
MH  - Melanocytes/*chemistry/ultrastructure
MH  - *Membrane Glycoproteins
MH  - Molecular Weight
MH  - Mutation
MH  - *Oxidoreductases
MH  - Pigmentation/genetics
MH  - Proteins/*analysis/genetics/physiology
MH  - Rabbits
MH  - gp100 Melanoma Antigen
EDAT- 1996/04/01 00:00
MHDA- 1996/04/01 00:01
CRDT- 1996/04/01 00:00
PHST- 1996/04/01 00:00 [pubmed]
PHST- 1996/04/01 00:01 [medline]
PHST- 1996/04/01 00:00 [entrez]
AID - S0022-202X(15)42501-1 [pii]
AID - 10.1111/1523-1747.ep12345163 [doi]
PST - ppublish
SO  - J Invest Dermatol. 1996 Apr;106(4):605-10. doi: 10.1111/1523-1747.ep12345163.