Regulation by GH of insulin-like growth factor-I mRNA expression in rat epiphyseal growth plate as studied with in-situ hybridization

Nilsson, Anders; Carlsson, Björn; Isgaard, Jörgen; Isaksson, Olle; Rymo, Lars

doi:10.1677/joe.0.1250067

Cited by 105 publications

(47 citation statements)

References 23 publications

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“…Until now, there have been conflicting reports whether both the IGFs are expressed in the postnatal epiphyseal growth plate. Expression of IGF-I was shown in the rat epiphyseal growth plate (P10, P28, P35) (Nilsson et al 1990, Reinecke et al 2000 and costochondral growth plate (Lin & Oberbauer 1999). In contrast, Wang et al (1995) detected only IGF-II in murine growth plates (P25) and Shinar et al (1993) reported similar results in rat growth plates (P10-P35).…”

Section: Discussionmentioning

confidence: 78%

“…Although species differences and age variables will influence the observed expression signals, the conflicting data are more likely caused by the detection method used. In previous studies (Nilsson et al 1990, Shinar et al 1993, Wang et al 1995, in which radioactive in situ hybridization was used, less clear expression of IGF-I and IGF-II was found. This was confirmed by Reinecke et al (2000), who also showed a better visible signal of IGF-I expression using non-radioactive in situ hybridization than that shown previously by the radioactive method (Nilsson et al 1990).…”

Section: Discussionmentioning

confidence: 89%

“…However, there still exists some doubt as to whether both IGF-I and IGF-II are produced in the growth plate. Several in vitro data have shown expression of both IGFs (Bhaumick 1993, Olney & Mougey 1999, while several in vivo studies have shown conflicting results (Nilsson et al 1990, Shinar et al 1993, Wang et al 1995, de los Rios & Hill 1999, Reinecke et al 2000.…”

Section: Introductionmentioning

confidence: 99%

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IGF and IGF-binding protein expression in the growth plate of normal, dexamethasone-treated and human IGF-II transgenic mice

Smink¹,

Koster²,

Gresnigt³

et al. 2002

Journal of Endocrinology

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Glucocorticoid (GC) treatment in childhood can lead to suppression of longitudinal growth as a side effect. The actions of GCs are thought to be mediated in part by impaired action of the insulin-like growth factors (IGF-I and IGF-II) and their binding proteins (IGFBP-1 to -6). We have studied the effects of GCs on IGF and IGFBP expression at the local level of the growth plate, using non-radioactive in situ hybridization.We treated 3-week-old normal mice for 4 weeks with dexamethasone (DXM). We also treated human IGF-II (hIGF-II) transgenic mice in order to investigate whether IGF-II could protect against the growth retarding effect of this GC. DXM treatment resulted in general growth retardation in both mice strains, however, only in normal mice was tibial length decreased. In both normal and hIGF-II trangenic mice, the total width of the growth plate was not affected, whereas the width of the proliferative zone decreased as a result of the DXM treatment. Additionally, only in normal mice, the width of the hypertrophic zone thickened.Only expression of IGF-I, IGF-II and IGFBP-2 could be detected in the growth plates of 7-week-old normal mice. IGFBP-1, -3, -4, -5 and -6 mRNAs were not detected. DXM treatment of normal mice induced a significant 2·4-fold increase in the number of cells expressing IGF-I mRNA, whereas IGF-II and IGFBP-2 mRNA levels were not affected.In hIGF-II transgenic mice, IGF-I mRNA levels were significantly increased, while endogenous IGF-II and IGFBP-2 mRNAs were unaffected, compared to normal animals. DXM treatment of the hIGF-II transgenic mice induced a further increase of IGF-I mRNA expression, to a similar extent as in DXM-treated normal mice.The increase of IGF-I due to DXM treatment in normal mice might be a reaction in order to minimize the GC-induced growth retardation. Another possibility could be that the increase of IGF-I would contribute to the GC-induced growth retardation by accelerating the differentiation of chondrocytes, resulting in accelerated ossification. In the growth plates of hIGF-II transgenic mice, the higher basal level of IGF-I, might be responsible for the observed partial protection against the adverse effects of GCs on bone.

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Section: Discussionmentioning

confidence: 78%

Section: Discussionmentioning

confidence: 89%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

IGF and IGF-binding protein expression in the growth plate of normal, dexamethasone-treated and human IGF-II transgenic mice

Smink¹,

Koster²,

Gresnigt³

et al. 2002

Journal of Endocrinology

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“…IGF-I is expressed by proliferating chondrocytes and osteoblasts within the growth plate as well as osteophyte [26,28]. It has an anabolic effect on cell proliferation and synthesis of collagen or matrix proteins in chondrocytes as well as in osteoblasts [13,24,32,36].…”

Section: K O K U X K I Et Al I Journul Ofmentioning

confidence: 99%

Expression of parathyroid hormone‐related peptide and insulin‐like growth factor I during rat fracture healing

Okazaki

Jingushi

Ikenoue

et al. 2003

Journal Orthopaedic Research

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Parathyroid hormone-related peptide (PTHrP) and insulin-like growth factor I (IGF-I) are both involved in the regulation of bone and cartilage metabolisms and their interaction has been reported in osteoblasts. To investigate the interaction of PTHrP and IGF-I during fracture healing, the expression of mRNA for PTHrP and IGF-I, and receptors for PTHlPTHrP and IGF were examined during rat femoral fracture healing using an in situ hybridization method and an immunohistochemistry method, respectively. During intramembranous ossification, PTHrP mRNA, IGF-I mRNA and IGF receptors were detected in preosteoblasts, differentiated osteoblasts and osteocytes in the newly formed trabecular bone. PTHlPTHrP receptors were markedly detected in osteoblasts and osteocytes, but only barely so in preosteoblasts. During cartilaginous callus formation, PTHrP mRNA was expressed by mesenchymal cells and proliferating chondrocytes. PTHlPTHrP receptors were detected in proliferating chondrocytes and early hypertrophic chondrocytes. IGF-I mRNA and IGF receptor were co-expressed by mesenchymal cells, proliferating chondrocytes, and early hypertrophic chondrocytes. At the endochondral ossification front, osteoblasts were positive for PTHrP and IGF-I mRNA as well as their receptors. These results suggest that IGF-I is involved in cell proliferation or differentiation in mesenchymal cells, periosteal cells, osteoblasts and chondrocytes in an autocrine andlor paracrine fashion. Furthermore, PTHrP may be involved in primary callus formation presumably co-operating with IGF-I in osteoblasts and osteocytes, and by regulating chondrocyte differentiation in endochondral ossification. IntroductionDuring fracture healing, several cellular events occur simultaneously and/or sequentially: inflammatory reaction, chondrogenesis, intramembranous ossification and endochondral ossification, resulting in the formation of a fracture callus followed by bony union. These dynamic events of bone metabolism are biologically regulated and can be investigated representatively in animal fracture models [15]. It has been reported that various local regulators such as cytokines and growth factors are expressed during fracture healing suggesting they regulate proliferation and/or differentiation of cells involved in fracture healing [11,39]. Since many growth factors regulate biological reaction of cells in co-operation with other factors or modulate the function of other factors [9,10,36], these interaction between different local regulators may be important for the well-organized repair process of fracture healing.Parathyroid hormone-related peptide (PTHrP) was originally isolated from tumors associated with humoral hypercalcemia of malignancy [34]. It has been reported that PTHrP is expressed in a wide variety of fetal and neonatal tissues [8,37], and acts in an autocrine/paracrine fashion binding with the same receptor as parathyroid hormone (PTH) does [16]. During embryonal cartilage development, PTHrP is expressed in the perichondrium induced by Indian ...

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“…Previous studies have demonstrated that a steady or daily growth factor action would be advantageous [35][36][37][38] and that 10 ng/mL IGF-1 is sufficient to stimulate the proliferative and metabolic activity of chondrocytes cultured in vitro, 39 while proteoglycan production is at a maximum with 100 ng/mL IGF-1. 40 The addition of IGF-1 to explants and monolayer cultures at concentrations of 10-200 ng/mL increased collagen type II and DNA synthesis and inhibited proteoglycan degradation, 41 whereas 200 ng/mL also inhibited chondrocyte apoptosis in vitro.…”

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confidence: 99%

Binding and Release Characteristics of Insulin-Like Growth Factor-1 from a Collagen–Glycosaminoglycan Scaffold

Mullen

Best

Brooks

et al. 2010

Tissue Engineering Part C: Methods

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Tissue engineering is a promising technique for cartilage repair, but to optimize novel scaffolds before clinical trials, it is necessary to determine their characteristics for binding and release of growth factors. Toward this goal, a novel, porous collagen-glycosaminoglycan scaffold was loaded with a range of concentrations of insulinlike growth factor-1 (IGF-1) to evaluate its potential as a controlled delivery device. The kinetics of IGF-1 adsorption and release from the scaffold was demonstrated using radiolabeled IGF-1. Adsorption was rapid, and was approximately proportional to the loading concentration. Ionic bonding contributed to this interaction. IGF-1 release was studied over 14 days to compare the release profiles from different loading groups. Two distinct phases occurred: first, a burst release of up to 44% was noted within the first 24 h; then, a slow, sustained release (13%-16%) was observed from day 1 to 14. When the burst release was subtracted, the relative percentage of remaining IGF-1 released was similar for all loading groups and broadly followed t ½ kinetics until approximately day 6. Scaffold cross-linking using dehydrothermal treatment did not affect IGF-1 adsorption or release. Bioactivity of released IGF-1 was confirmed by seeding scaffolds (preadsorbed with unlabeled IGF-1) with human osteoarthritic chondrocytes and demonstrating increased proteoglycan production in vitro.

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Regulation by GH of insulin-like growth factor-I mRNA expression in rat epiphyseal growth plate as studied with in-situ hybridization

Cited by 105 publications

References 23 publications

IGF and IGF-binding protein expression in the growth plate of normal, dexamethasone-treated and human IGF-II transgenic mice

IGF and IGF-binding protein expression in the growth plate of normal, dexamethasone-treated and human IGF-II transgenic mice

Expression of parathyroid hormone‐related peptide and insulin‐like growth factor I during rat fracture healing

Binding and Release Characteristics of Insulin-Like Growth Factor-1 from a Collagen–Glycosaminoglycan Scaffold

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