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Hideki Kishimura - One of the best experts on this subject based on the ideXlab platform.
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characteristics of Acid and pepsin soluble collagens from scale of seabass lates calcarifer
Lwt - Food Science and Technology, 2015Co-Authors: Sira Chuaychan, Hideki KishimuraAbstract:Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from seabass (Lates calcarifer) scale were characterised. Yields of ASC and PSC were 0.38 and 1.06% (based on dry weight), respectively. Both ASC and PSC were identified to be type I collagen, which consisted of α1 and α2 chains. β component was also found in both collagens. ASC and PSC contained glycine as the major amino Acid and had high Imino Acid content (193–198 residues/1000 residues). Tmax of ASC and PSC from seabass scale were 38.17 °C and 39.32 °C, respectively. FTIR spectra indicated that triple helical structure of resulting PSC was not disrupted by pepsin digestion. ASC and PSC from seabass scale exhibited high solubility in very Acidic pH range (pH 2–4). Therefore, seabass scale could be an alternative source of collagen and the characteristics of collagens were slightly affected by extraction process used.
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characteristics of collagens from the swim bladders of yellowfin tuna thunnus albacares
Food Chemistry, 2014Co-Authors: Onouma Kaewdang, Thammarat Kaewmanee, Hideki KishimuraAbstract:Abstract Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were extracted from the swim bladders of yellowfin tuna ( Thunnus albacares ) with yields of 1.07% and 12.10%, respectively. Based on electrophoretic patterns, both ASC and PSC consisted of two α-chains (α1 and α2) and were characterised to be type I collagen. ASC had higher β-chains than PSC. Imino Acid contents of ASC and PSC were 128 and 169 residues/1000 residues, respectively. Fourier transform infrared (FTIR) spectra of both ASC and PSC were similar and revealed the presence of a triple helix. Both ASC and PSC had the highest solubility at Acidic pHs. From zeta potential analysis, a net charge of zero was found at pH 6.05 and 5.93 for ASC and PSC, respectively. T max of ASC and PSC were 32.97 and 33.92 °C, respectively. The swim bladders of yellowfin tuna could therefore serve as an alternative source of collagen for future applications.
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characteristics and gel properties of gelatin from skin of seabass lates calcarifer as influenced by extraction conditions
Food Chemistry, 2014Co-Authors: Sittichoke Sinthusamran, Soottawat Benjakul, Hideki KishimuraAbstract:Characteristics and gel properties of gelatin from seabass skin, as influenced by extraction conditions, were studied. Yields of gelatin extracted at 45 and 55 °C for various times were 51.6–57.3% and 62.0–66.4% (dry weight basis), respectively. All gelatins contained β-chain and α-chains as the predominant components and showed a high Imino Acid content (198–202 residues/1000 residues). Generally, the gel strength of gelatins decreased as the extraction temperature and time increased. Gelatin extracted at 45 °C for 3 h exhibited the highest gel strength (369 g). Gelling and melting temperatures for seabass skin gelatin were 19.5–20.0 and 26.3–27.0 °C, respectively. All gelatins could be set at 25 °C within 30 min, however gelatins extracted at 45 °C had a shorter setting time than those extracted at 55 °C (P < 0.05). Gelatin from seabass skin showed a higher gel strength than bovine gelatin and could be used as a potential replacement for land animal gelatins.
Maria A Schumacher - One of the best experts on this subject based on the ideXlab platform.
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crystal structure of human type iii collagen gly991 gly1032 cystine knot containing peptide shows both 7 2 and 10 3 triple helical symmetries
Journal of Biological Chemistry, 2008Co-Authors: Sergei P Boudko, Jurgen Engel, Kenji Okuyama, Kazunori Mizuno, Hans Peter Bachinger, Maria A SchumacherAbstract:Abstract Type III collagen is a critical collagen that comprises extensible connective tissue such as skin, lung, and the vascular system. Mutations in the type III collagen gene, COL3A1, are associated with the most severe forms of Ehlers-Danlos syndrome. A characteristic feature of type III collagen is the presence of a stabilizing C-terminal cystine knot. Crystal structures of collagen triple helices reported so far contain artificial sequences like (Gly-Pro-Pro)n or (Gly-Pro-Hyp)n. To gain insight into the structural properties exhibited by the natural type III collagen triple helix, we synthesized, crystallized, and determined the structure of a 12-triplet repeating peptide containing the natural type III collagen sequence from residues 991 to 1032 including the C-terminal cystine knot region, to 2.3A resolution. This represents the longest collagen triple helical structure determined to date with a native sequence. Strikingly, the Gly991–Gly1032 structure reveals that the central non-Imino Acid-containing region adopts 10/3 superhelical properties, whereas the Imino Acid rich N- and C-terminal regions adhere to a 7/2 superhelical conformation. The structure is consistent with two models for the cystine knot; however, the poor density for the majority of this region suggests that multiple conformations may be adopted. The structure shows that the multiple non-Imino Acids make several types of direct intrahelical as well as interhelical contacts. The looser superhelical structure of the non-Imino Acid region of collagen triple helices combined with the extra contacts afforded by ionic and polar residues likely play a role in fibrillar assembly and interactions with other extracellular components.
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Crystal Structure of Human Type III Collagen Gly991–Gly1032 Cystine Knot-containing Peptide Shows Both 7/2 and 10/3 Triple Helical Symmetries
The Journal of biological chemistry, 2008Co-Authors: Sergei P Boudko, Jurgen Engel, Kenji Okuyama, Kazunori Mizuno, Hans Peter Bachinger, Maria A SchumacherAbstract:Type III collagen is a critical collagen that comprises extensible connective tissue such as skin, lung, and the vascular system. Mutations in the type III collagen gene, COL3A1, are associated with the most severe forms of Ehlers-Danlos syndrome. A characteristic feature of type III collagen is the presence of a stabilizing C-terminal cystine knot. Crystal structures of collagen triple helices reported so far contain artificial sequences like (Gly-Pro-Pro)(n) or (Gly-Pro-Hyp)(n). To gain insight into the structural properties exhibited by the natural type III collagen triple helix, we synthesized, crystallized, and determined the structure of a 12-triplet repeating peptide containing the natural type III collagen sequence from residues 991 to 1032 including the C-terminal cystine knot region, to 2.3A resolution. This represents the longest collagen triple helical structure determined to date with a native sequence. Strikingly, the Gly(991)-Gly(1032) structure reveals that the central non-Imino Acid-containing region adopts 10/3 superhelical properties, whereas the Imino Acid rich N- and C-terminal regions adhere to a 7/2 superhelical conformation. The structure is consistent with two models for the cystine knot; however, the poor density for the majority of this region suggests that multiple conformations may be adopted. The structure shows that the multiple non-Imino Acids make several types of direct intrahelical as well as interhelical contacts. The looser superhelical structure of the non-Imino Acid region of collagen triple helices combined with the extra contacts afforded by ionic and polar residues likely play a role in fibrillar assembly and interactions with other extracellular components.
Catriona M. H. Anderson - One of the best experts on this subject based on the ideXlab platform.
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deciphering the mechanisms of intestinal Imino and amino Acid transport the redemption of slc36a1
Biochimica et Biophysica Acta, 2007Co-Authors: David T Thwaites, Catriona M. H. AndersonAbstract:The absorption of zwitterionic Imino and amino Acids, and related drugs, is an essential function of the small intestinal epithelium. This review focuses on the physiological roles of transporters recently identified at the molecular level, in particular SLC36A1, by identifying how they relate to the classical epithelial Imino and amino Acid transporters characterised in mammalian small intestine in the 1960s-1990s. SLC36A1 transports a number of D- and L-Imino and amino Acids, beta- and gamma-amino Acids and orally-active neuromodulatory and antibacterial agents. SLC36A1 (or PAT1) functions as a proton-coupled Imino and amino Acid symporter in cooperation with the Na+/H+ exchanger NHE3 (SLC9A3) to produce the Imino Acid carrier identified in rat small intestine in the 1960s but subsequently ignored because of confusion with the Imino transporter. However, it is the sodium/Imino and amino Acid cotransporter SLC6A20 which corresponds to the betaine carrier (identified in hamster, 1960s) and Imino transporter (identified in rabbit and guinea pig, 1980s). This review summarises evidence for expression of SLC36A1 and SLC6A20 in human small intestine, highlights the differences in functional characteristics of the Imino Acid carrier and Imino transporter, and explains the confusion surrounding these two distinct transport systems.
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h amino Acid transporter 1 pat1 is the Imino Acid carrier an intestinal nutrient drug transporter in human and rat
Gastroenterology, 2004Co-Authors: Catriona M. H. Anderson, Danielle S. Grenade, Michael Boll, Martin Foltz, Katherine A. Wake, David J. Kennedy, Lars Munck, Seiji Miyauchi, Peter M. Taylor, Frederick Charles CampbellAbstract:Background & Aims: Amino Acid (and related drug) absorption across the human small intestinal wall is an essential intestinal function. Despite the revelation of a number of mammalian genomes, the molecular identity of the classic Na + -dependent Imino Acid transporter (identified functionally in the 1960s) remains elusive. The aims of this study were to determine whether the recently isolated complementary DNA hPAT1 (human proton-coupled amino Acid transporter 1), or solute carrier SLC36A1, represents the Imino Acid carrier; the Na + -dependent Imino Acid transport function measured at the brush-border membrane of intact intestinal epithelia results from a close functional relationship between human proton-coupled amino Acid transporter-1 and Na + /H + exchanger 3 (NHE3). Methods: PAT1 function was measured in isolation ( Xenopus laevis oocytes) and in intact epithelia (Caco-2 cell monolayers and rat small intestine) by measurement of amino Acid and/or H + influx. Tissue and membrane expression of PAT1 were determined by reverse-transcription polymerase chain reaction and immunohistochemistry. Results: PAT1-specific immunofluorescence was localized exclusively to the luminal membrane of Caco-2 cells and human and rat small intestine. The substrate specificity of hPAT1 is identical to that of the Imino Acid carrier. In intact epithelia, PAT1-mediated amino Acid influx is reduced under conditions in which NHE3 is inactive. Conclusions: The identification in intact epithelia of a cooperative functional relationship between PAT1 (H + /amino Acid symport) and NHE3 (Na + /H + exchange) explains the apparent Na + dependence of the Imino Acid carrier in studies with mammalian intestine. hPAT1 is the high-capacity Imino Acid carrier localized at the small intestinal luminal membrane that transports nutrients (Imino/amino Acids) and orally active neuromodulatory agents (used to treat affective disorders).
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H+/amino Acid transporter 1 (PAT1) is the Imino Acid carrier: An intestinal nutrient/drug transporter in human and rat.
Gastroenterology, 2004Co-Authors: Catriona M. H. Anderson, Danielle S. Grenade, Michael Boll, Martin Foltz, Katherine A. Wake, David J. Kennedy, Lars Munck, Seiji Miyauchi, Peter M. Taylor, Frederick Charles CampbellAbstract:Background & Aims: Amino Acid (and related drug) absorption across the human small intestinal wall is an essential intestinal function. Despite the revelation of a number of mammalian genomes, the molecular identity of the classic Na + -dependent Imino Acid transporter (identified functionally in the 1960s) remains elusive. The aims of this study were to determine whether the recently isolated complementary DNA hPAT1 (human proton-coupled amino Acid transporter 1), or solute carrier SLC36A1, represents the Imino Acid carrier; the Na + -dependent Imino Acid transport function measured at the brush-border membrane of intact intestinal epithelia results from a close functional relationship between human proton-coupled amino Acid transporter-1 and Na + /H + exchanger 3 (NHE3). Methods: PAT1 function was measured in isolation ( Xenopus laevis oocytes) and in intact epithelia (Caco-2 cell monolayers and rat small intestine) by measurement of amino Acid and/or H + influx. Tissue and membrane expression of PAT1 were determined by reverse-transcription polymerase chain reaction and immunohistochemistry. Results: PAT1-specific immunofluorescence was localized exclusively to the luminal membrane of Caco-2 cells and human and rat small intestine. The substrate specificity of hPAT1 is identical to that of the Imino Acid carrier. In intact epithelia, PAT1-mediated amino Acid influx is reduced under conditions in which NHE3 is inactive. Conclusions: The identification in intact epithelia of a cooperative functional relationship between PAT1 (H + /amino Acid symport) and NHE3 (Na + /H + exchange) explains the apparent Na + dependence of the Imino Acid carrier in studies with mammalian intestine. hPAT1 is the high-capacity Imino Acid carrier localized at the small intestinal luminal membrane that transports nutrients (Imino/amino Acids) and orally active neuromodulatory agents (used to treat affective disorders).
Frederick Charles Campbell - One of the best experts on this subject based on the ideXlab platform.
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h amino Acid transporter 1 pat1 is the Imino Acid carrier an intestinal nutrient drug transporter in human and rat
Gastroenterology, 2004Co-Authors: Catriona M. H. Anderson, Danielle S. Grenade, Michael Boll, Martin Foltz, Katherine A. Wake, David J. Kennedy, Lars Munck, Seiji Miyauchi, Peter M. Taylor, Frederick Charles CampbellAbstract:Background & Aims: Amino Acid (and related drug) absorption across the human small intestinal wall is an essential intestinal function. Despite the revelation of a number of mammalian genomes, the molecular identity of the classic Na + -dependent Imino Acid transporter (identified functionally in the 1960s) remains elusive. The aims of this study were to determine whether the recently isolated complementary DNA hPAT1 (human proton-coupled amino Acid transporter 1), or solute carrier SLC36A1, represents the Imino Acid carrier; the Na + -dependent Imino Acid transport function measured at the brush-border membrane of intact intestinal epithelia results from a close functional relationship between human proton-coupled amino Acid transporter-1 and Na + /H + exchanger 3 (NHE3). Methods: PAT1 function was measured in isolation ( Xenopus laevis oocytes) and in intact epithelia (Caco-2 cell monolayers and rat small intestine) by measurement of amino Acid and/or H + influx. Tissue and membrane expression of PAT1 were determined by reverse-transcription polymerase chain reaction and immunohistochemistry. Results: PAT1-specific immunofluorescence was localized exclusively to the luminal membrane of Caco-2 cells and human and rat small intestine. The substrate specificity of hPAT1 is identical to that of the Imino Acid carrier. In intact epithelia, PAT1-mediated amino Acid influx is reduced under conditions in which NHE3 is inactive. Conclusions: The identification in intact epithelia of a cooperative functional relationship between PAT1 (H + /amino Acid symport) and NHE3 (Na + /H + exchange) explains the apparent Na + dependence of the Imino Acid carrier in studies with mammalian intestine. hPAT1 is the high-capacity Imino Acid carrier localized at the small intestinal luminal membrane that transports nutrients (Imino/amino Acids) and orally active neuromodulatory agents (used to treat affective disorders).
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H+/amino Acid transporter 1 (PAT1) is the Imino Acid carrier: An intestinal nutrient/drug transporter in human and rat.
Gastroenterology, 2004Co-Authors: Catriona M. H. Anderson, Danielle S. Grenade, Michael Boll, Martin Foltz, Katherine A. Wake, David J. Kennedy, Lars Munck, Seiji Miyauchi, Peter M. Taylor, Frederick Charles CampbellAbstract:Background & Aims: Amino Acid (and related drug) absorption across the human small intestinal wall is an essential intestinal function. Despite the revelation of a number of mammalian genomes, the molecular identity of the classic Na + -dependent Imino Acid transporter (identified functionally in the 1960s) remains elusive. The aims of this study were to determine whether the recently isolated complementary DNA hPAT1 (human proton-coupled amino Acid transporter 1), or solute carrier SLC36A1, represents the Imino Acid carrier; the Na + -dependent Imino Acid transport function measured at the brush-border membrane of intact intestinal epithelia results from a close functional relationship between human proton-coupled amino Acid transporter-1 and Na + /H + exchanger 3 (NHE3). Methods: PAT1 function was measured in isolation ( Xenopus laevis oocytes) and in intact epithelia (Caco-2 cell monolayers and rat small intestine) by measurement of amino Acid and/or H + influx. Tissue and membrane expression of PAT1 were determined by reverse-transcription polymerase chain reaction and immunohistochemistry. Results: PAT1-specific immunofluorescence was localized exclusively to the luminal membrane of Caco-2 cells and human and rat small intestine. The substrate specificity of hPAT1 is identical to that of the Imino Acid carrier. In intact epithelia, PAT1-mediated amino Acid influx is reduced under conditions in which NHE3 is inactive. Conclusions: The identification in intact epithelia of a cooperative functional relationship between PAT1 (H + /amino Acid symport) and NHE3 (Na + /H + exchange) explains the apparent Na + dependence of the Imino Acid carrier in studies with mammalian intestine. hPAT1 is the high-capacity Imino Acid carrier localized at the small intestinal luminal membrane that transports nutrients (Imino/amino Acids) and orally active neuromodulatory agents (used to treat affective disorders).
Sergei P Boudko - One of the best experts on this subject based on the ideXlab platform.
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crystal structure of human type iii collagen gly991 gly1032 cystine knot containing peptide shows both 7 2 and 10 3 triple helical symmetries
Journal of Biological Chemistry, 2008Co-Authors: Sergei P Boudko, Jurgen Engel, Kenji Okuyama, Kazunori Mizuno, Hans Peter Bachinger, Maria A SchumacherAbstract:Abstract Type III collagen is a critical collagen that comprises extensible connective tissue such as skin, lung, and the vascular system. Mutations in the type III collagen gene, COL3A1, are associated with the most severe forms of Ehlers-Danlos syndrome. A characteristic feature of type III collagen is the presence of a stabilizing C-terminal cystine knot. Crystal structures of collagen triple helices reported so far contain artificial sequences like (Gly-Pro-Pro)n or (Gly-Pro-Hyp)n. To gain insight into the structural properties exhibited by the natural type III collagen triple helix, we synthesized, crystallized, and determined the structure of a 12-triplet repeating peptide containing the natural type III collagen sequence from residues 991 to 1032 including the C-terminal cystine knot region, to 2.3A resolution. This represents the longest collagen triple helical structure determined to date with a native sequence. Strikingly, the Gly991–Gly1032 structure reveals that the central non-Imino Acid-containing region adopts 10/3 superhelical properties, whereas the Imino Acid rich N- and C-terminal regions adhere to a 7/2 superhelical conformation. The structure is consistent with two models for the cystine knot; however, the poor density for the majority of this region suggests that multiple conformations may be adopted. The structure shows that the multiple non-Imino Acids make several types of direct intrahelical as well as interhelical contacts. The looser superhelical structure of the non-Imino Acid region of collagen triple helices combined with the extra contacts afforded by ionic and polar residues likely play a role in fibrillar assembly and interactions with other extracellular components.
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Crystal Structure of Human Type III Collagen Gly991–Gly1032 Cystine Knot-containing Peptide Shows Both 7/2 and 10/3 Triple Helical Symmetries
The Journal of biological chemistry, 2008Co-Authors: Sergei P Boudko, Jurgen Engel, Kenji Okuyama, Kazunori Mizuno, Hans Peter Bachinger, Maria A SchumacherAbstract:Type III collagen is a critical collagen that comprises extensible connective tissue such as skin, lung, and the vascular system. Mutations in the type III collagen gene, COL3A1, are associated with the most severe forms of Ehlers-Danlos syndrome. A characteristic feature of type III collagen is the presence of a stabilizing C-terminal cystine knot. Crystal structures of collagen triple helices reported so far contain artificial sequences like (Gly-Pro-Pro)(n) or (Gly-Pro-Hyp)(n). To gain insight into the structural properties exhibited by the natural type III collagen triple helix, we synthesized, crystallized, and determined the structure of a 12-triplet repeating peptide containing the natural type III collagen sequence from residues 991 to 1032 including the C-terminal cystine knot region, to 2.3A resolution. This represents the longest collagen triple helical structure determined to date with a native sequence. Strikingly, the Gly(991)-Gly(1032) structure reveals that the central non-Imino Acid-containing region adopts 10/3 superhelical properties, whereas the Imino Acid rich N- and C-terminal regions adhere to a 7/2 superhelical conformation. The structure is consistent with two models for the cystine knot; however, the poor density for the majority of this region suggests that multiple conformations may be adopted. The structure shows that the multiple non-Imino Acids make several types of direct intrahelical as well as interhelical contacts. The looser superhelical structure of the non-Imino Acid region of collagen triple helices combined with the extra contacts afforded by ionic and polar residues likely play a role in fibrillar assembly and interactions with other extracellular components.
