1.Insulin-like Growth Factors and Nutrition.
Journal of the Korean Pediatric Society 2001;44(3):235-241
No abstract available.
Somatomedins*
2.The Role of Insulin-Like Growth Factors in Central Nervous System.
Journal of Korean Society of Pediatric Endocrinology 2000;5(1):28-34
No abstract available.
Central Nervous System*
;
Somatomedins*
3.Insulin-like Growth Factors and Dermatosis.
Hong Yan TANG ; Bin XIAO ; Li Ping WANG ; Gui Lan YANG
Acta Academiae Medicinae Sinicae 2019;41(3):415-418
Insulin-like growth factors(IGFs)are polypeptides structurally homologous to insulin.By binding to membrane tyrosine receptors,they regulate the proliferation,differentiation,apoptosis,growth,and development of body cells and are involved in the pathogenesis of tumors and other diseases.In recent years,more research on IGFs of dermatosis increased.This article reviews recent research advances in IGFs and its relationship with dermatosis.
Humans
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Peptides
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Skin Diseases
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Somatomedins
4.Plasma somatomedin C levels in normal children.
Jung Tak KIM ; Ho Seong KIM ; Duk Hi KIM
Journal of the Korean Pediatric Society 1992;35(11):1493-1500
No abstract available.
Child*
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Humans
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Insulin-Like Growth Factor I*
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Plasma*
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Somatomedins*
6.Research progress on the influence mechanism of insulin like growth factors system on growth restriction.
Acta Academiae Medicinae Sinicae 2011;33(1):18-21
Insulin-like growth factors (IGF) system plays an important role in regulating growth and development of children. The change of this system is closely related to growth restriction caused by various diseases. This article reviews the research progress on how IGF system affects growth.
Developmental Disabilities
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metabolism
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physiopathology
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Humans
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Somatomedins
;
metabolism
;
physiology
7.Research on expression of somatomedin b domain of proteoglycan 4 and recombinant protein aggregation.
Lifang WANG ; Zhibo HAN ; Wenhu CHEN ; Peng DU ; Aihua SUN ; Ping YANG ; Hongguang ZHAO
Journal of Biomedical Engineering 2014;31(6):1319-1324
Recombinant protein SMB(PRG4) containing two Somatomedin B domains and a small amount of glycosylation of repetitive sequences of proteoglycan 4 was cloned according to PGR4 gene polymorphism. Mature purification process was established and recombinant protein SMB(PRG4), with high-level expression was purified. By using size-exclusion chromatogaraphy and dynamic light scattering, we found that the recombinant protein self-aggregate to dimeric form. Structure prediction and non-reducing electrophoresis revealed that SMB(PRG4), was a non-covalently bonded dimer.
Glycosylation
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Protein Multimerization
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Proteoglycans
;
chemistry
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Recombinant Proteins
;
chemistry
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Somatomedins
;
chemistry
8.Plasma Somatomedin in Children with Perthes' Disease
The Journal of the Korean Orthopaedic Association 1985;20(2):213-218
No abstract available in English.
Child
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Humans
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Legg-Calve-Perthes Disease
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Plasma
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Somatomedins
9.Growth hormone, somatomedin C levels in umbilical cord blood in premature, term, postterm neonates.
Kyung Ho LIM ; Myung Chul SHIN ; Yong Won PARK ; In Kyu KIM ; Chan Ho SONG
Korean Journal of Obstetrics and Gynecology 1993;36(7):1769-1774
No abstract available.
Fetal Blood*
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Growth Hormone*
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Humans
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Infant, Newborn*
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Insulin-Like Growth Factor I*
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Somatomedins*
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Umbilical Cord*
10.Biological roles of insulin-like growth factor binding proteins (IGFBPs).
Ho Seong KIM ; Ron G ROSENFELD ; Young Man OH
Experimental & Molecular Medicine 1997;29(2):85-96
The insulin-like growth factor binding protein (IGFBP) family is a critical component of the insulin-like growth factor (IGF) system which regulate the biological actions of the IGFs and may also be capable of IGF-independent actions. To date, seven distinct IGFBPs have been described. Among these IGFBPs, IGFBPs-1-6 bind IGFs with high affinity, while only IGFBP-7 binds with low affinity. Recently, we have demonstrated that connective tissue growth factor (CTGF) also binds IGFs with low affinity, suggesting that a family of low-affinity IGFBPs, distinct from the high-affinity members, may exist, and together these constitute an IGFBP superfamily. IGFBPs have various biological roles. IGFBPs act not only as a carrier proteins, but also as a modulators of IGF actions by involving in IGF ligand-receptor interactions through influences on both the bioavailability and distribution of IGFs in the extracellular environment. In addition, some IGFBPs (IGFBPs-1, -3, and -5) appears to have intrinsic activity independent of IGFs. This review will focus on recent studies on the biological roles of IGFBPs in IGF-dependent and IGF-independent modes.
Biological Availability
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Carrier Proteins
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Connective Tissue Growth Factor
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Humans
;
Insulin-Like Growth Factor Binding Proteins*
;
Somatomedins