Secretion of the vitamin K-dependent protein of bone by rat osteosarcoma cells. Evidence for an intracellular precursor

Satoru Nishimoto, P. A. Price

Research output: Contribution to journalArticle

128 Citations (Scopus)

Abstract

Four clonal cell lines derived from a rat osteosarcoma were tested for the ability to secrete the γ-carboxyglutamic acid-containing protein of bone (BGP) using a specific radioimmunoassay for this protein. Two cell lines secreted BGP into culture media while the other two did not. Other investigators have shown that these two cell lines are also the only ones with the high parathyroid hormone responsiveness and alkaline phosphatase activity expected for osteoblast cells in culture. Both cell lines also form a mineralized sarcoma when implanted in rats. The BGP in culture media is identical in molecular weight and in electrophoretic mobility with the 5800-dalton BGP purified from rat bone. Thus, BGP is probably secreted by osteosarcoma cells directly and not derived from an extracellular precursor by proteolytic cleavage. There are two immunoreactive components within osteosarcoma cells which secrete BGP. One component is identical in molecular weight and electrophoretic mobility with BGP from rat bone. The other component has a higher molecular mass (approximately 9000 daltons) and about half the electrophoretic mobility of BGP from bone. The presence of both components within these cells raises the possibility that the larger component may be an intracellular precursor which is processed to BGP prior to secretion.

Original languageEnglish (US)
Pages (from-to)6579-6583
Number of pages5
JournalJournal of Biological Chemistry
Volume255
Issue number14
StatePublished - 1980
Externally publishedYes

Fingerprint

Osteocalcin
Osteosarcoma
Electrophoretic mobility
Rats
Bone
Cells
Bone and Bones
Cell Line
Culture Media
Molecular Weight
Molecular weight
Osteoblasts
Molecular mass
Cellular Structures
Parathyroid Hormone
Cell culture
Sarcoma
Radioimmunoassay
Alkaline Phosphatase
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Secretion of the vitamin K-dependent protein of bone by rat osteosarcoma cells. Evidence for an intracellular precursor. / Nishimoto, Satoru; Price, P. A.

In: Journal of Biological Chemistry, Vol. 255, No. 14, 1980, p. 6579-6583.

Research output: Contribution to journalArticle

@article{7e7be976f1e745c2a82a75b2e1369ac2,
title = "Secretion of the vitamin K-dependent protein of bone by rat osteosarcoma cells. Evidence for an intracellular precursor",
abstract = "Four clonal cell lines derived from a rat osteosarcoma were tested for the ability to secrete the γ-carboxyglutamic acid-containing protein of bone (BGP) using a specific radioimmunoassay for this protein. Two cell lines secreted BGP into culture media while the other two did not. Other investigators have shown that these two cell lines are also the only ones with the high parathyroid hormone responsiveness and alkaline phosphatase activity expected for osteoblast cells in culture. Both cell lines also form a mineralized sarcoma when implanted in rats. The BGP in culture media is identical in molecular weight and in electrophoretic mobility with the 5800-dalton BGP purified from rat bone. Thus, BGP is probably secreted by osteosarcoma cells directly and not derived from an extracellular precursor by proteolytic cleavage. There are two immunoreactive components within osteosarcoma cells which secrete BGP. One component is identical in molecular weight and electrophoretic mobility with BGP from rat bone. The other component has a higher molecular mass (approximately 9000 daltons) and about half the electrophoretic mobility of BGP from bone. The presence of both components within these cells raises the possibility that the larger component may be an intracellular precursor which is processed to BGP prior to secretion.",
author = "Satoru Nishimoto and Price, {P. A.}",
year = "1980",
language = "English (US)",
volume = "255",
pages = "6579--6583",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "14",

}

TY - JOUR

T1 - Secretion of the vitamin K-dependent protein of bone by rat osteosarcoma cells. Evidence for an intracellular precursor

AU - Nishimoto, Satoru

AU - Price, P. A.

PY - 1980

Y1 - 1980

N2 - Four clonal cell lines derived from a rat osteosarcoma were tested for the ability to secrete the γ-carboxyglutamic acid-containing protein of bone (BGP) using a specific radioimmunoassay for this protein. Two cell lines secreted BGP into culture media while the other two did not. Other investigators have shown that these two cell lines are also the only ones with the high parathyroid hormone responsiveness and alkaline phosphatase activity expected for osteoblast cells in culture. Both cell lines also form a mineralized sarcoma when implanted in rats. The BGP in culture media is identical in molecular weight and in electrophoretic mobility with the 5800-dalton BGP purified from rat bone. Thus, BGP is probably secreted by osteosarcoma cells directly and not derived from an extracellular precursor by proteolytic cleavage. There are two immunoreactive components within osteosarcoma cells which secrete BGP. One component is identical in molecular weight and electrophoretic mobility with BGP from rat bone. The other component has a higher molecular mass (approximately 9000 daltons) and about half the electrophoretic mobility of BGP from bone. The presence of both components within these cells raises the possibility that the larger component may be an intracellular precursor which is processed to BGP prior to secretion.

AB - Four clonal cell lines derived from a rat osteosarcoma were tested for the ability to secrete the γ-carboxyglutamic acid-containing protein of bone (BGP) using a specific radioimmunoassay for this protein. Two cell lines secreted BGP into culture media while the other two did not. Other investigators have shown that these two cell lines are also the only ones with the high parathyroid hormone responsiveness and alkaline phosphatase activity expected for osteoblast cells in culture. Both cell lines also form a mineralized sarcoma when implanted in rats. The BGP in culture media is identical in molecular weight and in electrophoretic mobility with the 5800-dalton BGP purified from rat bone. Thus, BGP is probably secreted by osteosarcoma cells directly and not derived from an extracellular precursor by proteolytic cleavage. There are two immunoreactive components within osteosarcoma cells which secrete BGP. One component is identical in molecular weight and electrophoretic mobility with BGP from rat bone. The other component has a higher molecular mass (approximately 9000 daltons) and about half the electrophoretic mobility of BGP from bone. The presence of both components within these cells raises the possibility that the larger component may be an intracellular precursor which is processed to BGP prior to secretion.

UR - http://www.scopus.com/inward/record.url?scp=0019309862&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0019309862&partnerID=8YFLogxK

M3 - Article

C2 - 6967067

AN - SCOPUS:0019309862

VL - 255

SP - 6579

EP - 6583

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 14

ER -