Localization of neutral, magnesium-stimulated sphingomyelinase in plasma membrane of cultured neuroblastoma cells

Matthew W. Spence; Jan Wakkary; Joe T.R. Clarke; Harold W. Cook

doi:10.1016/0304-4165(82)90321-X

Localization of neutral, magnesium-stimulated sphingomyelinase in plasma membrane of cultured neuroblastoma cells

Matthew W. Spence, Jan Wakkary, Joe T.R. Clarke, Harold W. Cook

Medicine

Producción científica: Contribución a una revista › Artículo › revisión exhaustiva

36 Citas (Scopus)

Resumen

A parallel is shown between the distribution of neutral sphingomyelinase and plasma membrane enzymes (5′-nucleotidase and (Na⁺ + K⁺)-activated ATPase) in cultured neuroblastoma cells. In contrast there is no evidence of localization in lysosomes (β-hexosaminidase and acid sphingomyelinase), mitochondria (carnitine palmitoyltransferase), or cytosol. Activity in the microsomal fraction is attributed primarily to plasma membrane contamination.

Idioma original	English
Páginas (desde-hasta)	162-164
Número de páginas	3
Publicación	Biochimica et Biophysica Acta - General Subjects
Volumen	719
N.º	1
DOI	https://doi.org/10.1016/0304-4165(82)90321-X
Estado	Published - oct. 28 1982

Nota bibliográfica

Funding Information:
The authors acknowledge the expert technical assistance of Mr. Alfred Archibald and Mr. Robert Zwicker. This research was supported in part by a grant-in-aid from the Medical Research Council of Canada (PG-16). H.W.C. is a Scholar and M.W.S. is a Career Investigator of the Medical Research Council of Canada.

ASJC Scopus Subject Areas

Biophysics
Biochemistry
Molecular Biology

Acceder al documento

10.1016/0304-4165(82)90321-X

Otros archivos y enlaces

Citar esto

@article{920fe7e952ce4b6080a7c74fcd02511d,

title = "Localization of neutral, magnesium-stimulated sphingomyelinase in plasma membrane of cultured neuroblastoma cells",

abstract = "A parallel is shown between the distribution of neutral sphingomyelinase and plasma membrane enzymes (5′-nucleotidase and (Na+ + K+)-activated ATPase) in cultured neuroblastoma cells. In contrast there is no evidence of localization in lysosomes (β-hexosaminidase and acid sphingomyelinase), mitochondria (carnitine palmitoyltransferase), or cytosol. Activity in the microsomal fraction is attributed primarily to plasma membrane contamination.",

author = "Spence, {Matthew W.} and Jan Wakkary and Clarke, {Joe T.R.} and Cook, {Harold W.}",

note = "Funding Information: The authors acknowledge the expert technical assistance of Mr. Alfred Archibald and Mr. Robert Zwicker. This research was supported in part by a grant-in-aid from the Medical Research Council of Canada (PG-16). H.W.C. is a Scholar and M.W.S. is a Career Investigator of the Medical Research Council of Canada.",

year = "1982",

month = oct,

day = "28",

doi = "10.1016/0304-4165(82)90321-X",

language = "English",

volume = "719",

pages = "162--164",

journal = "Biochimica et Biophysica Acta - General Subjects",

issn = "0304-4165",

publisher = "Elsevier",

number = "1",

}

TY - JOUR

T1 - Localization of neutral, magnesium-stimulated sphingomyelinase in plasma membrane of cultured neuroblastoma cells

AU - Spence, Matthew W.

AU - Wakkary, Jan

AU - Clarke, Joe T.R.

AU - Cook, Harold W.

N1 - Funding Information: The authors acknowledge the expert technical assistance of Mr. Alfred Archibald and Mr. Robert Zwicker. This research was supported in part by a grant-in-aid from the Medical Research Council of Canada (PG-16). H.W.C. is a Scholar and M.W.S. is a Career Investigator of the Medical Research Council of Canada.

PY - 1982/10/28

Y1 - 1982/10/28

N2 - A parallel is shown between the distribution of neutral sphingomyelinase and plasma membrane enzymes (5′-nucleotidase and (Na+ + K+)-activated ATPase) in cultured neuroblastoma cells. In contrast there is no evidence of localization in lysosomes (β-hexosaminidase and acid sphingomyelinase), mitochondria (carnitine palmitoyltransferase), or cytosol. Activity in the microsomal fraction is attributed primarily to plasma membrane contamination.

AB - A parallel is shown between the distribution of neutral sphingomyelinase and plasma membrane enzymes (5′-nucleotidase and (Na+ + K+)-activated ATPase) in cultured neuroblastoma cells. In contrast there is no evidence of localization in lysosomes (β-hexosaminidase and acid sphingomyelinase), mitochondria (carnitine palmitoyltransferase), or cytosol. Activity in the microsomal fraction is attributed primarily to plasma membrane contamination.

UR - http://www.scopus.com/inward/record.url?scp=0020381423&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020381423&partnerID=8YFLogxK

U2 - 10.1016/0304-4165(82)90321-X

DO - 10.1016/0304-4165(82)90321-X

M3 - Article

C2 - 6293585

AN - SCOPUS:0020381423

SN - 0304-4165

VL - 719

SP - 162

EP - 164

JO - Biochimica et Biophysica Acta - General Subjects

JF - Biochimica et Biophysica Acta - General Subjects

IS - 1

ER -

Localization of neutral, magnesium-stimulated sphingomyelinase in plasma membrane of cultured neuroblastoma cells

Resumen

Nota bibliográfica

ASJC Scopus Subject Areas

Acceder al documento

Otros archivos y enlaces

Huella

Citar esto