Laminin isoforms in human embryonic stem cells : synthesis, receptor usage and growth support

Vuoristo, Sanna; Virtanen, Ismo; Takkunen, Minna; Palgi, Jaan; Kikkawa, Yamato; Rousselle, Patricia; Sekiguchi, Kiyotoshi; Tuuri, Timo; Otonkoski, Timo

doi:https://doi.org/10.1111/j.1582-4934.2008.00643.x

Laminin isoforms in human embryonic stem cells : synthesis, receptor usage and growth support

Vuoristo, Sanna; Virtanen, Ismo; Takkunen, Minna et al.

Journal of Cellular and Molecular Medicine, 2009, 13(8b), 2622-2633

Number of Access:536（2025-08-18 14:33 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/71822

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Title	Laminin isoforms in human embryonic stem cells : synthesis, receptor usage and growth support
Creator	CreatorName Vuoristo, Sanna
	CreatorName Virtanen, Ismo
	CreatorName Takkunen, Minna
	CreatorName Palgi, Jaan
	NRID 1000020274227 1000020274227 CreatorName Kikkawa, Yamato
	CreatorName Rousselle, Patricia
	NRID 1000050187845 1000050187845 researchmap permalink read0054833 read0054833 Scopus Author ID 7201662709 7201662709 ORCID 0000-0002-6433-1410 0000-0002-6433-1410 CreatorName Sekiguchi, Kiyotoshi
	CreatorName Tuuri, Timo
	CreatorName Otonkoski, Timo
Subject	human embryonic stem cell
	extracellular matrix
	basement membrane
	laminin
	integrin
	B‐CAM/Lutheran
	adhesion
	defined cultures
Description	Sanna Vuoristo, Ismo Virtanen, Minna Takkunen, Jaan Palgi, Yamato Kikkawa, Patricia Rousselle, Kiyotoshi Sekiguchi, Timo Tuuri, and Timo Otonkoski, "Laminin isoforms in human embryonic stem cells: synthesis, receptor usage and growth support", Journal of Cellular and Molecular Medicine, 13, 8b, pp. 2622-2633, Wiley, 2009
Abstract	To reveal the functional intrinsic niche of human embryonic stem cells (hESC) we examined the production of basement membrane (BM) proteins and the presence of their receptors in feeder‐free cell culture conditions. In addition, we investigated binding of hESCs to purified human BM proteins and identified the receptors mediating these contacts. Also, we tested whether purified human laminin (Lm) isoforms have a role in hESC self‐renewal and growth in short‐term cultures. The results show that hESCs synthesize Lm α1 and Lm α5 chains together with Lm β1 and γ1 chains suggesting the production of Lms‐111 and ‐511 into the culture medium and deposits on cells. hESCs contain functionally important integrin (Int) subunits, Int β1, α3, α6, α5, β5 and αV, as well as the Lm α5 receptor, Lutheran (Lu) glycoprotein and its truncated form, basal cell adhesion molecule (B‐CAM). In cell adhesion experiments, Int β1 was crucial for adhesion to most of the purified human BM proteins. Lu/B‐CAM mediated adhesion to Lm‐511 together with Int α3β1, and was essential for the adhesion of hESCs to embryonic feeder cells. Adhesion to Lm‐411 was mediated by Int α6β1. Lm‐511 supported hESC growth in defined medium equally well as Matrigel. These results provide consequential information of the biological role of BM in hESCs, warranting further investigation of BM biology of human pluripotent stem cells.
Publisher	Wiley
Source Title	Journal of Cellular and Molecular Medicine
Volume (Issue)	13(8b)
Page	2622-2633
Date of Issued	2009-08
Language	English
Handle URL	https://hdl.handle.net/11094/71822
eISSN	15824934
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1111/j.1582-4934.2008.00643.x
Access Rights	open access
CopyRight	© 2008 The Authors Journal compilation. © 2009 Foundation for Cellular and Molecular Medicine/Blackwell Publishing Ltd
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	Journal of Cellular and Molecular Medicine. 2009, 13(8b), p. 2622-2633
DC.title	Laminin isoforms in human embryonic stem cells : synthesis, receptor usage and growth support
DC.creator	Vuoristo, Sanna
	Virtanen, Ismo
	Takkunen, Minna
	Palgi, Jaan
	Kikkawa, Yamato
	Rousselle, Patricia
	Sekiguchi, Kiyotoshi
	Tuuri, Timo
	Otonkoski, Timo
DC.publisher	Wiley
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2009-08
DC.identifier	https://doi.org/10.1111/j.1582-4934.2008.00643.x
DC.subject	human embryonic stem cell
	extracellular matrix
	basement membrane
	laminin
	integrin
	B‐CAM/Lutheran
	adhesion
	defined cultures
DC.description	Sanna Vuoristo, Ismo Virtanen, Minna Takkunen, Jaan Palgi, Yamato Kikkawa, Patricia Rousselle, Kiyotoshi Sekiguchi, Timo Tuuri, and Timo Otonkoski, "Laminin isoforms in human embryonic stem cells: synthesis, receptor usage and growth support", Journal of Cellular and Molecular Medicine, 13, 8b, pp. 2622-2633, Wiley, 2009
DCTERMS.abstract	To reveal the functional intrinsic niche of human embryonic stem cells (hESC) we examined the production of basement membrane (BM) proteins and the presence of their receptors in feeder‐free cell culture conditions. In addition, we investigated binding of hESCs to purified human BM proteins and identified the receptors mediating these contacts. Also, we tested whether purified human laminin (Lm) isoforms have a role in hESC self‐renewal and growth in short‐term cultures. The results show that hESCs synthesize Lm α1 and Lm α5 chains together with Lm β1 and γ1 chains suggesting the production of Lms‐111 and ‐511 into the culture medium and deposits on cells. hESCs contain functionally important integrin (Int) subunits, Int β1, α3, α6, α5, β5 and αV, as well as the Lm α5 receptor, Lutheran (Lu) glycoprotein and its truncated form, basal cell adhesion molecule (B‐CAM). In cell adhesion experiments, Int β1 was crucial for adhesion to most of the purified human BM proteins. Lu/B‐CAM mediated adhesion to Lm‐511 together with Int α3β1, and was essential for the adhesion of hESCs to embryonic feeder cells. Adhesion to Lm‐411 was mediated by Int α6β1. Lm‐511 supported hESC growth in defined medium equally well as Matrigel. These results provide consequential information of the biological role of BM in hESCs, warranting further investigation of BM biology of human pluripotent stem cells.
DC.rights	© 2008 The Authors Journal compilation. © 2009 Foundation for Cellular and Molecular Medicine/Blackwell Publishing Ltd
DC.format	71822
citation_title	Laminin isoforms in human embryonic stem cells : synthesis, receptor usage and growth support
citation_author	Vuoristo, Sanna
	Virtanen, Ismo
	Takkunen, Minna
	Palgi, Jaan
	Kikkawa, Yamato
	Rousselle, Patricia
	Sekiguchi, Kiyotoshi
	Tuuri, Timo
	Otonkoski, Timo
citation_publisher	Wiley
citation_language	English
citation_date	2009-08
citation_journal_title	Journal of Cellular and Molecular Medicine
citation_volume	13
citation_issue	8b
citation_firstpage	2622
citation_lastpage	2633
citation_doi	https://doi.org/10.1111/j.1582-4934.2008.00643.x
citation_public_url	https://hdl.handle.net/11094/71822

Laminin isoforms in human embryonic stem cells : synthesis, receptor usage and growth support

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