Characteristics of rat pancreatic regenerating protein

M. E. Zenilman, J. Chen, B. Danesh, Q. H. Zheng

Research output: Contribution to journalArticle

Abstract

Background. The pancreatic regenerating (reg) gene is an acinar cell product involved in islet formation and maintenance. Human reg protein is mitogenic to pancreatic beta and ductular cells, and its amino acid sequence predicts it to be a calcium-dependent lectin. Methods. We studied the biologic activity and cellular localization of rat reg I isolated from the acinar cell line AR42J and the lectin properties of reg from AR42J and pancreatic juice. Bioactivity was assayed by milogenesis on the ductular cell line ARIP. Cellular localization was determined by differential centrifugation. Lectin properties were assessed by affinity chromatography. Results. Reg protein from crude AR42J cellular lysate and purified reg protein from AR42J induced thymidine incorporation to ARIP Conditioned medium from AR42J and co-culture of AR42J with morphologically distinguishable ARIP, however, failed to induce mitogenesis. Reg protein was localized within the vesicle fraction of the cell and was not membrane bound. Affinity chromotography revealed that reg protein did not bind to mannose or galactose in the presence or absence of calcium. In pancreatic juice a previously undescribed mannose-binding protein was discovered at 25,000 to 30,000 daltons. Conclusions. We conclude that reg produced in the acinar cell line AR42J is biologically active but not efficiently secreted, even though it localized within the cellular vesicles. Despite predictions based on its amino acid sequence, it does not appear to be a calcium-dependent lectin.

Original languageEnglish (US)
Pages (from-to)855-863
Number of pages9
JournalSurgery
Volume124
Issue number5
StatePublished - 1998
Externally publishedYes

Fingerprint

Lectins
Acinar Cells
Pancreatic Juice
Proteins
Calcium
Cell Line
Amino Acid Sequence
Mannose-Binding Lectin
Insulin-Secreting Cells
Mannose
Conditioned Culture Medium
Coculture Techniques
Galactose
Centrifugation
Affinity Chromatography
Thymidine
Maintenance
rat Reg1 protein
Membranes
Genes

ASJC Scopus subject areas

  • Surgery

Cite this

Zenilman, M. E., Chen, J., Danesh, B., & Zheng, Q. H. (1998). Characteristics of rat pancreatic regenerating protein. Surgery, 124(5), 855-863.

Characteristics of rat pancreatic regenerating protein. / Zenilman, M. E.; Chen, J.; Danesh, B.; Zheng, Q. H.

In: Surgery, Vol. 124, No. 5, 1998, p. 855-863.

Research output: Contribution to journalArticle

Zenilman, ME, Chen, J, Danesh, B & Zheng, QH 1998, 'Characteristics of rat pancreatic regenerating protein', Surgery, vol. 124, no. 5, pp. 855-863.
Zenilman ME, Chen J, Danesh B, Zheng QH. Characteristics of rat pancreatic regenerating protein. Surgery. 1998;124(5):855-863.
Zenilman, M. E. ; Chen, J. ; Danesh, B. ; Zheng, Q. H. / Characteristics of rat pancreatic regenerating protein. In: Surgery. 1998 ; Vol. 124, No. 5. pp. 855-863.
@article{dc25ea5e3b854383a8c6084e41c5a83c,
title = "Characteristics of rat pancreatic regenerating protein",
abstract = "Background. The pancreatic regenerating (reg) gene is an acinar cell product involved in islet formation and maintenance. Human reg protein is mitogenic to pancreatic beta and ductular cells, and its amino acid sequence predicts it to be a calcium-dependent lectin. Methods. We studied the biologic activity and cellular localization of rat reg I isolated from the acinar cell line AR42J and the lectin properties of reg from AR42J and pancreatic juice. Bioactivity was assayed by milogenesis on the ductular cell line ARIP. Cellular localization was determined by differential centrifugation. Lectin properties were assessed by affinity chromatography. Results. Reg protein from crude AR42J cellular lysate and purified reg protein from AR42J induced thymidine incorporation to ARIP Conditioned medium from AR42J and co-culture of AR42J with morphologically distinguishable ARIP, however, failed to induce mitogenesis. Reg protein was localized within the vesicle fraction of the cell and was not membrane bound. Affinity chromotography revealed that reg protein did not bind to mannose or galactose in the presence or absence of calcium. In pancreatic juice a previously undescribed mannose-binding protein was discovered at 25,000 to 30,000 daltons. Conclusions. We conclude that reg produced in the acinar cell line AR42J is biologically active but not efficiently secreted, even though it localized within the cellular vesicles. Despite predictions based on its amino acid sequence, it does not appear to be a calcium-dependent lectin.",
author = "Zenilman, {M. E.} and J. Chen and B. Danesh and Zheng, {Q. H.}",
year = "1998",
language = "English (US)",
volume = "124",
pages = "855--863",
journal = "Surgery",
issn = "0039-6060",
publisher = "Mosby Inc.",
number = "5",

}

TY - JOUR

T1 - Characteristics of rat pancreatic regenerating protein

AU - Zenilman, M. E.

AU - Chen, J.

AU - Danesh, B.

AU - Zheng, Q. H.

PY - 1998

Y1 - 1998

N2 - Background. The pancreatic regenerating (reg) gene is an acinar cell product involved in islet formation and maintenance. Human reg protein is mitogenic to pancreatic beta and ductular cells, and its amino acid sequence predicts it to be a calcium-dependent lectin. Methods. We studied the biologic activity and cellular localization of rat reg I isolated from the acinar cell line AR42J and the lectin properties of reg from AR42J and pancreatic juice. Bioactivity was assayed by milogenesis on the ductular cell line ARIP. Cellular localization was determined by differential centrifugation. Lectin properties were assessed by affinity chromatography. Results. Reg protein from crude AR42J cellular lysate and purified reg protein from AR42J induced thymidine incorporation to ARIP Conditioned medium from AR42J and co-culture of AR42J with morphologically distinguishable ARIP, however, failed to induce mitogenesis. Reg protein was localized within the vesicle fraction of the cell and was not membrane bound. Affinity chromotography revealed that reg protein did not bind to mannose or galactose in the presence or absence of calcium. In pancreatic juice a previously undescribed mannose-binding protein was discovered at 25,000 to 30,000 daltons. Conclusions. We conclude that reg produced in the acinar cell line AR42J is biologically active but not efficiently secreted, even though it localized within the cellular vesicles. Despite predictions based on its amino acid sequence, it does not appear to be a calcium-dependent lectin.

AB - Background. The pancreatic regenerating (reg) gene is an acinar cell product involved in islet formation and maintenance. Human reg protein is mitogenic to pancreatic beta and ductular cells, and its amino acid sequence predicts it to be a calcium-dependent lectin. Methods. We studied the biologic activity and cellular localization of rat reg I isolated from the acinar cell line AR42J and the lectin properties of reg from AR42J and pancreatic juice. Bioactivity was assayed by milogenesis on the ductular cell line ARIP. Cellular localization was determined by differential centrifugation. Lectin properties were assessed by affinity chromatography. Results. Reg protein from crude AR42J cellular lysate and purified reg protein from AR42J induced thymidine incorporation to ARIP Conditioned medium from AR42J and co-culture of AR42J with morphologically distinguishable ARIP, however, failed to induce mitogenesis. Reg protein was localized within the vesicle fraction of the cell and was not membrane bound. Affinity chromotography revealed that reg protein did not bind to mannose or galactose in the presence or absence of calcium. In pancreatic juice a previously undescribed mannose-binding protein was discovered at 25,000 to 30,000 daltons. Conclusions. We conclude that reg produced in the acinar cell line AR42J is biologically active but not efficiently secreted, even though it localized within the cellular vesicles. Despite predictions based on its amino acid sequence, it does not appear to be a calcium-dependent lectin.

UR - http://www.scopus.com/inward/record.url?scp=0031774785&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031774785&partnerID=8YFLogxK

M3 - Article

C2 - 9823399

AN - SCOPUS:0031774785

VL - 124

SP - 855

EP - 863

JO - Surgery

JF - Surgery

SN - 0039-6060

IS - 5

ER -