The NGF and kallikrein genes of mouse, the African rat Mastomys natalensis and man: their distribution and mode of expression in the salivary gland

Bowcock, Anne M.; Fahnestock, Margaret; Goslin, K; Shooter, Eric M.

doi:10.1016/0169-328x(88)90062-9

Cited by 12 publications

(5 citation statements)

References 26 publications

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“…Proteolytic cleavage at the C-terminus of p-NGF may be peculiar to 7s complex formation in the mouse salivary glands. Although p-NGF is typically found associated with high molecular weight complexes, the 7s complex has been unequivocally detected only in mouse saliva and salivary glands (Bowcock et al, 1988;Darling and Fahnestock, 1988;Drinkwater et al, 1988;Schwarz et al, 1989). There is no information concerning the exact size of P-NGF (i.e., 118 versus 120 amino acids) synthesized in the CNS.…”

Section: I991mentioning

confidence: 99%

Physicochemical Characterization of Recombinant Human Nerve Growth Factor Produced in Insect Cells with a Baculovirus Vector

Barnett

Chow

Nguyen

et al. 1991

Journal of Neurochemistry

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Recombinant human nerve growth factor (rhNGF) secreted by insect cells was purified by ion-exchange and reversed-phase chromatography to near homogeneity. The N-terminus of the secreted molecule was analogous to that of mouse salivary gland NGF. In its native conformation, the insect cell produced rhNGF molecules were homodimers consisting of 120 amino acid polypeptide chains. Mature rhNGF was found not to be significantly glycosylated (less than 0.08 mol of N-acetylglucosamine/mol of protein). The rhNGF was homogeneous with regard to molecular weight and amino acid sequence. Isoelectric focusing resolved the rhNGF into one major and one minor component. Because rhNGF from insect cells can be obtained in large quantities, purified to near homogeneity, and is similar to natural NGF with regard to physicochemical properties and biological activity, it is suitable for further evaluation in animal models as a therapeutic molecule for neurodegenerative diseases such as Alzheimer's disease.

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Section: I991mentioning

confidence: 99%

Physicochemical Characterization of Recombinant Human Nerve Growth Factor Produced in Insect Cells with a Baculovirus Vector

Barnett

Chow

Nguyen

et al. 1991

Journal of Neurochemistry

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“…Salivary constituents have a number of biological functions, which in some ways are keys to maintaining oral health. Saliva has been recognized as a rich source of growth factors such as epidermal growth factor (EGF) and nerve growth factor (NGF) (2). EGF has hormone‐like properties and consists of 53 amino acids (3).…”

mentioning

confidence: 99%

Physiologic levels of Epidermal Growth Factor in saliva stimulate cell migration of an oral epithelial cell line, HO‐1‐N‐1

Ohshima

Sato

Ishikawa

et al. 2002

European J Oral Sciences

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An oral epithelial cell line derived from buccal mucosa squamous cell carcinoma, HO-1-N-1, was used to elucidate the role of epidermal growth factor (EGF) in saliva on wound healing of the oral mucosa. The effects of EGF on DNA synthesis, and cell migration was studied and the related signal transduction pathways examined. DNA synthesis by HO-1-N-1 cells was stimulated dose-dependently by 1-10 ng ml(-1) EGF, but significantly inhibited by addition of a PI3-K inhibitor (wortmannin), a p38 MAPK inhibitor (SB203580) or an MEKs inhibitor (PD98059). Cell migration was also accelerated by addition of 1-10 ng ml(-1) EGF; however, the migration rate was decreased to 30% by adding PD98059, to 40% by adding a tyrosine kinase inhibitor (herbimycin A), and to 60% by adding wortmannin or dexamethasone. These results indicate that the physiologic concentration of EGF in saliva may stimulate proliferation and migration of oral epithelial cells for wound healing, when the oral mucosa has been injured. Furthermore, this study revealed that EGF-stimulated signal transduction pathways for epithelial cell proliferation and cell migration are different.

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“…A large family of enzymes with TK-related sequences has been detected in the mouse with as many as 24 to 25 genes, of which 10 to 14 are functional (Mason et al, 1983;Evans et al, 1987;Berg et al, 1992). A similar large number of 11 to 17 genes has been described in the rat (Wines et al, 1991), and in the African rat Mastomys (Bowcock et al, 1988). It has been suggested that these enzymes, differing in substrate specificities, are functionally important because of their ability to selectively cleave very many specific polypeptide precursors of bioactive peptides (Mason et al, 1983;Bothwell et al, 1979).…”

Section: Introductionmentioning

confidence: 84%

“…Large TK multigene families have been identified only in the rat (Wines et al, 1991), mouse (Evans et al, 1987;Berg et al, 1992), and the African rat Mastomys (Bowcock et al, 1988), which are closely related species. Similar multigene families comprising around 10 members have been reported for the trypsins of man (Emi et al, 1986), rat (Craik et al, 1984) and mouse (Stevenson et al, 1986).…”

Section: Discussionmentioning

confidence: 99%

Not More than Three Tissue Kallikreins Identified from Organs of the Guinea Pig

Fiedler¹,

Betz²,

Hinz³

et al. 1999

Biological Chemistry

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The large and varied multigene families of tissue kallikreins of rat and mouse are considered to selectively release as many bioactive peptides. In order to determine whether a similar family of enzymes is expressed in the organs of the guinea pig purification studies were performed. Tissue kallikreins from the submandibular gland, coagulating gland/prostate complex and the pancreas were separated by affinity chromatography on benzamidine-Sepharose. Amino-terminal sequences, the patterns of hydrolysis rates of a number of peptide p-nitroanilides, inactivation rates by active site-directed irreversible inhibitors, specific kininogenase activities and types of kinin released were used to probe the identity of the isolated enzymes.Guinea pig tissue kallikreins 1 and 2 have been reported previously. In the present study we have identified a third type, designated tissue kallikrein 1a because of its sequence similarity to kallikrein 1, which differs from the latter in the catalytic properties. The inferred occurrence of not more than two or three independent tissue kallikrein genes in the guinea pig contrasts with the varied family of enzymes expressed by the large number of such genes present in rats and mice. Expression in the guinea pig (and also in humans) of only a small number of tissue kallikreins makes specific processing of a multitude of biologically active peptides by such enzymes unlikely.

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The NGF and kallikrein genes of mouse, the African rat Mastomys natalensis and man: their distribution and mode of expression in the salivary gland

Cited by 12 publications

References 26 publications

Physicochemical Characterization of Recombinant Human Nerve Growth Factor Produced in Insect Cells with a Baculovirus Vector

Physicochemical Characterization of Recombinant Human Nerve Growth Factor Produced in Insect Cells with a Baculovirus Vector

Physiologic levels of Epidermal Growth Factor in saliva stimulate cell migration of an oral epithelial cell line, HO‐1‐N‐1

Not More than Three Tissue Kallikreins Identified from Organs of the Guinea Pig

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