Localization and characterization of a novel secreted protein SCUBE1 in human platelets

Cheng Fen Tu; Yueh Hsing Su; Ya Ni Huang; Ming Tzu Tsai; Li Tzu Li; Yuh Lien Chen; Chien Jui Cheng; Dao Fu Dai; Ruey Bing Yang

doi:10.1016/j.cardiores.2006.04.010

Localization and characterization of a novel secreted protein SCUBE1 in human platelets

Cheng Fen Tu, Yueh Hsing Su, Ya Ni Huang, Ming Tzu Tsai, Li Tzu Li, Yuh Lien Chen, Chien Jui Cheng, Dao Fu Dai, Ruey Bing Yang

Research output: Contribution to journal › Article › peer-review

88 Citations (Scopus)

Abstract

Objective: The aim of the study was to investigate the protein expression and function of a novel secreted protein in the vascular system, named SCUBE1 for signal peptide, CUB (Complement proteins C1r/C1s, Uegf, and Bmp1) and epidermal growth factor-like (EGF)-like domain containing protein 1. Methods and results: Immunohistochemical analysis demonstrated that the SCUBE1 staining is mainly confined to the intravascular platelet-rich thrombus in vascular tissue samples. While quantitative real-time RT-PCR verified that the SCUBE1 mRNA is expressed in human platelets, numerous immunolocalization techniques revealed that the preformed SCUBE1 protein is stored in the α-granules and translocated to the surface upon platelet stimulation. A smaller SCUBE1 fragment, possibly formed by limited proteolysis after being released from the storage granules, was detected in thrombus lysate by Western blot analysis. Interestingly, deposition of SCUBE1 into the subendothelial matrix of the atherosclerotic plaques was evidenced by immunohistochemistry. In addition, studies of platelet adhesion and ristocetin-induced platelet agglutination showed that fragments containing the amino-terminal EGF-like repeats were able to support platelet adhesion and enhance the ristocetin-induced platelet agglutination, respectively. Conclusion: These data suggest that platelet-derived SCUBE1 could function as a novel adhesive molecule and its matrix-bound and soluble fragments may play critical (patho)physiological roles in cardiovascular biology.

Original language	English
Pages (from-to)	486-495
Number of pages	10
Journal	Cardiovascular Research
Volume	71
Issue number	3
DOIs	https://doi.org/10.1016/j.cardiores.2006.04.010
Publication status	Published - Aug 1 2006

Keywords

Atherosclerosis
Electron microscopy
Extracellular matrix
Histo(patho)logy
Platelets

ASJC Scopus subject areas

Physiology
Cardiology and Cardiovascular Medicine
Physiology (medical)

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10.1016/j.cardiores.2006.04.010

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@article{9c4c4cb85cbe40b89bd4fecf7455bfab,

title = "Localization and characterization of a novel secreted protein SCUBE1 in human platelets",

abstract = "Objective: The aim of the study was to investigate the protein expression and function of a novel secreted protein in the vascular system, named SCUBE1 for signal peptide, CUB (Complement proteins C1r/C1s, Uegf, and Bmp1) and epidermal growth factor-like (EGF)-like domain containing protein 1. Methods and results: Immunohistochemical analysis demonstrated that the SCUBE1 staining is mainly confined to the intravascular platelet-rich thrombus in vascular tissue samples. While quantitative real-time RT-PCR verified that the SCUBE1 mRNA is expressed in human platelets, numerous immunolocalization techniques revealed that the preformed SCUBE1 protein is stored in the α-granules and translocated to the surface upon platelet stimulation. A smaller SCUBE1 fragment, possibly formed by limited proteolysis after being released from the storage granules, was detected in thrombus lysate by Western blot analysis. Interestingly, deposition of SCUBE1 into the subendothelial matrix of the atherosclerotic plaques was evidenced by immunohistochemistry. In addition, studies of platelet adhesion and ristocetin-induced platelet agglutination showed that fragments containing the amino-terminal EGF-like repeats were able to support platelet adhesion and enhance the ristocetin-induced platelet agglutination, respectively. Conclusion: These data suggest that platelet-derived SCUBE1 could function as a novel adhesive molecule and its matrix-bound and soluble fragments may play critical (patho)physiological roles in cardiovascular biology.",

keywords = "Atherosclerosis, Electron microscopy, Extracellular matrix, Histo(patho)logy, Platelets",

author = "Tu, {Cheng Fen} and Su, {Yueh Hsing} and Huang, {Ya Ni} and Tsai, {Ming Tzu} and Li, {Li Tzu} and Chen, {Yuh Lien} and Cheng, {Chien Jui} and Dai, {Dao Fu} and Yang, {Ruey Bing}",

note = "Funding Information: We thank Dr. Shyh-Chyi Lo for advice and help on platelet aggregation assay. This study was supported by Grant 91-B-FA09-2-4 from the Ministry of Education Program for Promoting Academic Excellence of Universities and National Science Council Grants NSC 93-2320-B-001-048, NSC 95-2752-B-006-003-PAE, and NSC 95-2752-B-001-002-PAE.",

year = "2006",

month = aug,

day = "1",

doi = "10.1016/j.cardiores.2006.04.010",

language = "English",

volume = "71",

pages = "486--495",

journal = "Cardiovascular Research",

issn = "0008-6363",

publisher = "Oxford University Press",

number = "3",

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TY - JOUR

T1 - Localization and characterization of a novel secreted protein SCUBE1 in human platelets

AU - Tu, Cheng Fen

AU - Su, Yueh Hsing

AU - Huang, Ya Ni

AU - Tsai, Ming Tzu

AU - Li, Li Tzu

AU - Chen, Yuh Lien

AU - Cheng, Chien Jui

AU - Dai, Dao Fu

AU - Yang, Ruey Bing

N1 - Funding Information: We thank Dr. Shyh-Chyi Lo for advice and help on platelet aggregation assay. This study was supported by Grant 91-B-FA09-2-4 from the Ministry of Education Program for Promoting Academic Excellence of Universities and National Science Council Grants NSC 93-2320-B-001-048, NSC 95-2752-B-006-003-PAE, and NSC 95-2752-B-001-002-PAE.

PY - 2006/8/1

Y1 - 2006/8/1

N2 - Objective: The aim of the study was to investigate the protein expression and function of a novel secreted protein in the vascular system, named SCUBE1 for signal peptide, CUB (Complement proteins C1r/C1s, Uegf, and Bmp1) and epidermal growth factor-like (EGF)-like domain containing protein 1. Methods and results: Immunohistochemical analysis demonstrated that the SCUBE1 staining is mainly confined to the intravascular platelet-rich thrombus in vascular tissue samples. While quantitative real-time RT-PCR verified that the SCUBE1 mRNA is expressed in human platelets, numerous immunolocalization techniques revealed that the preformed SCUBE1 protein is stored in the α-granules and translocated to the surface upon platelet stimulation. A smaller SCUBE1 fragment, possibly formed by limited proteolysis after being released from the storage granules, was detected in thrombus lysate by Western blot analysis. Interestingly, deposition of SCUBE1 into the subendothelial matrix of the atherosclerotic plaques was evidenced by immunohistochemistry. In addition, studies of platelet adhesion and ristocetin-induced platelet agglutination showed that fragments containing the amino-terminal EGF-like repeats were able to support platelet adhesion and enhance the ristocetin-induced platelet agglutination, respectively. Conclusion: These data suggest that platelet-derived SCUBE1 could function as a novel adhesive molecule and its matrix-bound and soluble fragments may play critical (patho)physiological roles in cardiovascular biology.

AB - Objective: The aim of the study was to investigate the protein expression and function of a novel secreted protein in the vascular system, named SCUBE1 for signal peptide, CUB (Complement proteins C1r/C1s, Uegf, and Bmp1) and epidermal growth factor-like (EGF)-like domain containing protein 1. Methods and results: Immunohistochemical analysis demonstrated that the SCUBE1 staining is mainly confined to the intravascular platelet-rich thrombus in vascular tissue samples. While quantitative real-time RT-PCR verified that the SCUBE1 mRNA is expressed in human platelets, numerous immunolocalization techniques revealed that the preformed SCUBE1 protein is stored in the α-granules and translocated to the surface upon platelet stimulation. A smaller SCUBE1 fragment, possibly formed by limited proteolysis after being released from the storage granules, was detected in thrombus lysate by Western blot analysis. Interestingly, deposition of SCUBE1 into the subendothelial matrix of the atherosclerotic plaques was evidenced by immunohistochemistry. In addition, studies of platelet adhesion and ristocetin-induced platelet agglutination showed that fragments containing the amino-terminal EGF-like repeats were able to support platelet adhesion and enhance the ristocetin-induced platelet agglutination, respectively. Conclusion: These data suggest that platelet-derived SCUBE1 could function as a novel adhesive molecule and its matrix-bound and soluble fragments may play critical (patho)physiological roles in cardiovascular biology.

KW - Atherosclerosis

KW - Electron microscopy

KW - Extracellular matrix

KW - Histo(patho)logy

KW - Platelets

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U2 - 10.1016/j.cardiores.2006.04.010

DO - 10.1016/j.cardiores.2006.04.010

M3 - Article

C2 - 16753137

AN - SCOPUS:33746321047

SN - 0008-6363

VL - 71

SP - 486

EP - 495

JO - Cardiovascular Research

JF - Cardiovascular Research

IS - 3

ER -

Localization and characterization of a novel secreted protein SCUBE1 in human platelets

Abstract

Keywords

ASJC Scopus subject areas

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