The Primary Structure of Epidermal Growth Factor

Savage, C. Richard; Inagami, Tadashi; Cohen, Stanley

doi:10.1016/s0021-9258(19)44569-9

Cited by 487 publications

(38 citation statements)

References 20 publications

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“…and present in many proteins of diverse function from invasion to postinvasion remodeling (Haynes et al, 1988;Adams et al, 1992) and cytoadherence (Su et al, 1997). Others include EGF (Savage et al, 1972) and six-cysteine (6-Cys) domains again implicated in protein-protein interactions (Ishino et al, 2005). The 6-Cys family is related to the surface antigen (SAG)-related sequence (SRS) superfamily found in coccidian members of the apicomplexan phylum (Gerloff et al, 2005;Arredondo et al, 2012).…”

Section: Molecules Functioning Directly In Invasionmentioning

confidence: 99%

The cellular and molecular basis for malaria parasite invasion of the human red blood cell

Cowman

Berry

Baum

2012

Journal of Cell Biology

328

294

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Malaria is a major disease of humans caused by protozoan parasites from the genus Plasmodium. It has a complex life cycle; however, asexual parasite infection within the blood stream is responsible for all disease pathology. This stage is initiated when merozoites, the free invasive blood-stage form, invade circulating erythrocytes. Although invasion is rapid, it is the only time of the life cycle when the parasite is directly exposed to the host immune system. Significant effort has, therefore, focused on identifying the proteins involved and understanding the underlying mechanisms behind merozoite invasion into the protected niche inside the human erythrocyte.

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Section: Molecules Functioning Directly In Invasionmentioning

confidence: 99%

The cellular and molecular basis for malaria parasite invasion of the human red blood cell

Cowman

Berry

Baum

2012

Journal of Cell Biology

328

294

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“…In the first synthetic step, EGF was activated with a large molar excess of glutaraldehyde to prevent dimer formation. Since EGF contains only one free amino group (26), a monoactivated EGF should be formed. In a control experiment, glutaraldehyde-activated EGF was chromatographed on the Bio-Gel A 1.5 m column.…”

Section: Characterization Of the E G F: Ferritin Synthetic Reactionmentioning

confidence: 99%

Direct visualization of the binding and internalization of a ferritin conjugate of epidermal growth factor in human carcinoma cells A-431.

Haigler¹,

McKanna²,

Cohen³

1979

The Journal of Cell Biology

510

272

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We have prepared a conjugate of epidermal growth factor (EGF) and ferritin that retains substantial binding affinity for cell receptors and is biologically active. Glutaraldehyde-activated EGF was covalently linked to ferritin to produce a conjugate that contained EGF and ferritin in a 1:1 molar ratio. The conjugate was separated from free ferritin by affinity chromatography using antibodies to EGF. Monolayers of human epithelioid carcinoma cells (A-431) were incubated with EGF:ferritin at 4~ and processed for transmission electron microscopy. Under these conditions, ~ 6 • 105 molecules of EGF:ferritin bound to the plasma membrane of each cell. In the presence of excess native EGF, the number of bound ferritin particles was reduced by 99%, indicating that EGF:ferritin binds specifically to cellular EGF receptors. At 37~ cell-bound EGF:ferritin rapidly redistributed in the plane of the plasma membrane to form small groups that were subsequently internalized into pinocytic vesicles. By 2.5 min at 37~ 32% of the cell-bound EGF:ferritin was localized in vesicles. After 2.5 min, there was a decrease in the proportion of conjugate in vesicles with a concomitant accumulation of EGF:ferritin in multivesicular bodies. By 30 min, 84% of the conjugate was located in structures morphologically identified as multivesicular bodies or lysosomes. These results are consistent with other morphological and biochemical studies utilizing I~I-EGF and fluorescein-conjugated EGF.KEY WORDS hormone receptors growth factor 9 endocytosis lysosomes Epidermal growth factor (EGF) ~ initiates a complex series of cellular events which ultimately 1 Abbreviations used in this paper: DMEM/BSA, Dulbecco's Modified Eagle Medium containing 0.1% bovine serum albumin; EGF, epidermal growth factor; I~I-EGF, l~ZI-labeled epidermal growth factor; MVB, multivesicular body; PBS, 9.5 mM sodium phosphate (pH 7.4) containing 4.14 mM KCI and 0.137 M NaCI.results in increased DNA synthesis and cell division (see references 6 and 7 for reviews). Cultured cells that are responsive to EGF contain specific, saturable plasma membrane receptors for this hormone (9, 19). As a first step in examining the biochemical mechanism by which EGF exerts its growth-promoting effects, we have investigated the metabolic fate of EGF using both ~I-labeled EGF and fluorescein-conjugated EGF. Our studies (4, 17) have indicated that cell-bound EGF rapidly is internalized into endocytic vesicles and 382J. CELL BIOLOGY 9 The Rockefeller University Press.

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“…A common feature of the EGF family members is that they are synthesized as larger transmembrane precursor molecules that can be cleaved proteolytically to release the soluble form of the growth factor or they can function as membrane-anchored growth factors in juxtacrine signalling. Members of the mammalian EGF family include EGF [2], transforming growth factor α (TGF-α) [3], heparinbinding EGF-like growth factor (HB-EGF) [4], epiregulin [5], amphiregulin (AR) [6], neural-and thymus-derived activator for ErbB kinases (' NTAK ') [7], the neuregulin subfamily, which includes the products of two alternately spliced genes NRG1 [8] and NRG2 [9,10] and a third gene, NRG3 [11], and betacellulin (BTC) [12].…”

Section: Introductionmentioning

confidence: 99%

Identification of betacellulin as a major peptide growth factor in milk: purification, characterization and molecular cloning of bovine betacellulin

Dunbar¹,

Priebe

Belford

et al. 1999

Biochem. J.

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Betacellulin (BTC), a member of the epidermal growth factor (EGF) family of peptide growth factors, was purified from a growth-factor-enriched whey fraction of bovine milk by a combination of ion-exchange chromatography, gel-filtration chromatography, affinity chromatography and reverse-phase HPLC. Bovine BTC (bBTC) had an apparent molecular mass of 21-22 kDa on SDS/PAGE and exists in a glycosylated form. The cDNA encoding bBTC was obtained by a combination of 5' and 3' rapid amplification of cDNA ends ('RACE'). The primary translation product consists of 178 amino acid residues containing a putative signal sequence, a transmembrane domain, the mature BTC domain and a cytoplasmic domain containing a highly hydrophilic Arg-Lys-rich region similar to that of mouse BTC and human BTC. The amino acid sequence of the bBTC precursor was 88% identical with human BTC and 79% identical with mouse BTC. The bBTC gene was found to be expressed in a wide range of tissues, including the mammary gland. The identification of BTC in milk raises the possibility that it has a major role in the growth and development of the neonatal gastrointestinal tract.

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The Primary Structure of Epidermal Growth Factor

Cited by 487 publications

References 20 publications

The cellular and molecular basis for malaria parasite invasion of the human red blood cell

The cellular and molecular basis for malaria parasite invasion of the human red blood cell

Direct visualization of the binding and internalization of a ferritin conjugate of epidermal growth factor in human carcinoma cells A-431.

Identification of betacellulin as a major peptide growth factor in milk: purification, characterization and molecular cloning of bovine betacellulin

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