• 제목/요약/키워드: proline-rich proteins

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구강점막 상피세포에 부착하는 타액 성분 (Salivary Components Adsorbing to Oral Mucosal Epithelial Cells)

  • 고홍섭
    • Journal of Oral Medicine and Pain
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    • 제24권3호
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    • pp.261-267
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    • 1999
  • The present investigation was carried out to identify salivary components of mucosal pellicle and to explore the difference of mucosal pellicle components according to the location of oral mucosa. By using antisera and immunoblotting, high-(MG1) and low-(MG2) molecular-mass salivary mucins, amylase, IgA, proline-rich proteins(PRPs) were detected in mucosal pellicle in vivo. In addition, the data indicated that mucins, IgA and proline-rich proteins could be cleaved into lower-molecular-mass products, whereas the IgA, proline-rich proteins could also be cross-linked into higher-molecular-mass complexes. Mucosal pellicles from buccal, labial and palatal mucosa showed similar pattern in immunoblotting experiments using anti-MG2 and anti-PRPs antisera. The data from this study suggest that during mucosal pellicle formation multiple components of saliva adsorb to oral mucosal epithelial cell surfaces, and selected components can be proteolytically cleaved into smaller fragments and/or cross-linked into higher-molecular products.

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사람의 타액선에서 proline-rich protein의 발현양상과 기능적 단백 구조에 대한 분자생물학적 연구 (A MOLECULAR BIOLOGICAL STUDY ON THE EXPRESSION PATTERN AND FUNCTIONAL PROTEIN STRUCTURES OF PROLINE-RICH PROTEINS IN HUMAN SALIVARY GLANDS)

  • 주재용;이석근;박영욱
    • Journal of the Korean Association of Oral and Maxillofacial Surgeons
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    • 제28권1호
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    • pp.31-41
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    • 2002
  • Proline-rich proteins (PRPs) are major components of human saliva. In order to know the biological roles of PRPs, we explored the expression pattern and functional protein structures of PRPs by the immunohistochemical and various molecular biological methods. Polyclonal antibody against human gPRP was generated from rabbit by the injection of oral exfoliated cells specially treated by urea and SDS buffer. The PRPs began to be expressed both in the acinar cells and ductal cells from the EIDS (Early Intermediate Developmental Stage) of fetal salivary glands and became intense in the salivary epithelium in the LDS (Late Developmental Stage) and adult salivary glands. The polyclonal antibody against the gPRP showed the cross-reactivity with aPRP and bPRP, these results were relevant to the high homology among subtypes of PRP. However, the simulated protein structures of PRPs showed the characteristic repetitive whorling domains except the N-terminal signal peptide. The whorling domains were also contained the multiple amino acids of glutamine and glycine, which may provide the receptor binding or cross-linking sites of PRPs.

Molecular interaction between SH3 domain of PACSIN2 and proline-rich motifs of Cobll1

  • Yoo, Hee-Seop;Seok, Seung-Hyeon;Kim, Ha-Neul;Kim, Ji-Hun;Seo, Min-Duk
    • 한국자기공명학회논문지
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    • 제26권3호
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    • pp.34-39
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    • 2022
  • The SH3 domain found within a variety of proteins is comprised of generally 60 residues, and participated in protein-protein interactions with proline-rich motifs. Cobll1 was identified as a distinct molecular marker associated with CML progression, and PACSIN2 was discovered a novel Cobll1 binding partner through direct interaction between a SH3 domain of PACSIN2 and three proline-rich motifs of Cobll1. To understand the structural basis of interactions between PACSIN2 and Cobll1, backbone assignments of PACSIN2 SH3 domain were performed. Furthermore, three proline-rich peptides of Cobll1 were titrated to 15N-labeled PACSIN2 SH3 domain in various ratios. Our chemical shift changes data and conserved SH3 sequence alignment will be helpful to analyze fundamental molecular basis related to the interaction between PACSIN2 and Cobll1.

Characteristics of Proline-rich Salivary Proteins Induced in Rat Parotid Glands by Tannins in Bean Hull

  • Kim, Hee-Seon
    • Nutritional Sciences
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    • 제2권2호
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    • pp.65-70
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    • 1999
  • Feeding rats a diet containing bean-hull causes hypertropy in their parotid glands due to the high tannin content. The amount of feedintake of rats led bean-hull was higher than that of rats fed a standard diet. However, the increase in body weight of rats fed bean-hull was lower than that of rats fed a standard diet, which resulted in significantly low feed efficiency of the bean-hull containing diet. Within one week, parotid glands significantly enlarged and a series of proline-rich proteins (PRPs) were produced, which were similar to those induced by feeding high-tannin sorghum with flight differences in molecular weights. Even though the direct comparison between PRPs produced by the bean-hull containing diet and those induced by the high sorghum diet is not appropriate due to laboratory inconsistences, several new PRPs were produced by high tannin diets in both experiments. Differences in molecular weights of PRPs induced in two different tannin sources must be funker investigated to be fully characterized. These morphological and biochemical changes have now been demonstrated to occur in response to the ingestion of tannins, presumably to diminish the anti-nutritional effects of tannins.

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악하선-설하선 혼합타액내 주요 단백질에 대한 구강내 주요 균주의 부착 (Adhesion of Oral Pathogens to Human Submandibular-Sublingual Salivary Proteins)

  • 이승우;정성창;김영구;고홍섭
    • Journal of Oral Medicine and Pain
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    • 제24권3호
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    • pp.235-244
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    • 1999
  • The present study was performed to investigate the binding between salivary proteins(low-molecular-weight mucin;MG2, amylase, proline-rich proteins;PRPs) and oral pathogens(Streptococcus gordonii, Actinomyces viscosus, Staphylococcus aureus) by using solid-phase assay. In the case of transferring proteins to Immobilon-P, S. gordonii binds to MG2. A. viscosus binds to MG2, amylase, and PRPs, and S. aureus binds to MG2 and amylase. On nitrocellulose membrane, S, gordonii and A. viscosus bind to MG2, amylase, and PRPs. S. aureus binds to MG2 and PRPs. However, rabbit anti-A. viscosus antisera and rabbit anti-S. aureus antisera showed cross reactivity to PRPs adsorbed to only nitrocellulose membrane in negative control experiments, which were done without bacterial overlay. The results were different according to the membrane used as solid-phase, which reflected the assay-sensitive nature of binding experiment. PRPs and amylase are known to be components of tooth enamel pellicle. In addition, there was experimental evidence that PRPs and MG2 may covalently bind to oral mucosal epithelium. Considering above facts, the results of the present study can provide information on the interactions between salivary proteins and oral bacteria on tooth and oral mucosal surfaces.

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타액내 혈형물질 분비형 및 비분비형에 따른 이하선 타액내 Pr,Db,Pa 단백질의 유전자 빈도 (The Gene Frequency in Parotid Salivary PR, DB, PA Proteins according to Salivary Secretory Blood Components)

  • San Kim;Chang-Lyuk Yoon
    • Journal of Oral Medicine and Pain
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    • 제19권2호
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    • pp.233-244
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    • 1994
  • The purpose of this study was to evaluate the gene frequency in parotid salivary proteins according to salivary blood components and salivary blood types. Parotid and whole saliva were collected from 160 healthy Korean adults (from 20 years of age to 43). They were divided by blood type(Q,B, AB,O type). Each group contained 40 adults respectively. They were tested to the salivary secretory blood components and parotid acidic protein(Pa), proline-rich protein(Pr) and double band protein(Db) were analyzed to evaluate the distribution of phenotype using alkaline slab polyacrylamide gel electrophoresis. Results were as follows : 1. In parotid saliva, the salivary blood substances were not found. In whole saliva, secretory type was 21.9% and non-secretory type was 78.1%. : In A type blood group, secretory type 87.5% and non-secretory type 12.5%. In B type blood group, secretory type 82.5% and non-secretory type 17.5%. In AB type blood group, secretory type 85% and non-secretory type 15%. In O type blood group, secretory type 57.5% and non-secretory type 42.5%. 2. The gene frequency of parotid acidic protein(Pa) were Pa+=0.160, Pa-=0.840 and proline-rich protein(Pr) were Pr1=0.781, Pr2=0.219 and double-band protein(Db) were Db+=0.019, Db-=0.981. 3. The difference between phenotype of Pa, Pr, Db proteins and salivary secretory blood components was not statistically significant. (P>0.05) 4. The difference between phenotype of Pa, Pr, Db proteins and blood types was not statistically significant.(P>0.05)

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인간 타액내 항 린산칼슘 침전 단백질 (Protein Inhibition Precipitation of Calcium Phosphate in Human Saliva)

  • Song Han
    • Journal of Oral Medicine and Pain
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    • 제20권1호
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    • pp.7-18
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    • 1995
  • The Purpose of this article is to describe the biochemical properties and biological functions of several salivary proteins that possess the unusual properties of inhibiting spontaneous and secondary precipitation of calcium phosphate. This function is very important since human salivary secretion is supersaturated with respect to calcium phosphate. Biological function of statherin, proline rich protein (PRP) and histidine rich protein (HRP) is to inhibit precipitation of calcium phosphate in salivary glands, in the oral fluids, and onto tooth surfaces. The resulting supersaturated state of the salivary secretions contributes a protective and reparative environment which is important for the integrity of the tooth. Beneficial consequences of salivary supersaturation with respect to calcium phosphate are selectively expressed in the oral cavity- that is, protection is provided for the dental enamel-while undesirable consequences, for example, precipitation of calcium phosphates in the salivary glands and onto the teeth do not occur. Purification and structural characteristics of these proteins as well as clinical significance of functions of each protein will be discussed.

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Molecular cloning and characterization of an antigenic protein with a repeating region from clonorchis sinensis

  • Kim, Tae-Yun;Kang, Shin-Yong;Ahn, Il-Young;Cho, Seung-Yull;Hong, Sung-Jong
    • Parasites, Hosts and Diseases
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    • 제39권1호
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    • pp.57-66
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    • 2001
  • In the course of immunoscreening of Clonorchis sinensis cDNA library, a cDNA CsRP12 containing a tandem repeat was isolated. The cDNA CsRP 12 encodes two putative peptides of open reading frames (ORFs) 1 and 2 (CsRP12-1 and -2). The repetitive region is composed of 15 repeats of 10 amino acids. Of the two putative peptides, CsRP12-1 was proline-rich and found to have homologues in several organisms. Recombinant proteins of the putative peptides were bacterially produced and purified by an affinity chromatography Recombinant CsRP12-1 protein was recognized by sera of clonorchiasis patients and experimental rabbits, but recombinant CsRP 12-2 was not. One of the putative peptide, CsRP12-1, is designated CsPRA, proline-rich antigen of C. sinensis. Both the C-termini of CsRP12-1 and -2 were bacterially produced and analysed to show no antigenicity. Recombinant CsPRA protein showed high sensitivity and specificity. In experimental rabbits, IgG antibodies to CsPRA was produced between 4 and 8 weeks after the infection and decreased thereafter over one you. These results indicate that CsPRA is equivalent to a natural protein and a useful antigenic protein for serodiagnosis of human clonorchiasis.

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인체 타액내 당단백질의 구조와 기능 (Structure and Function of Glycoproteins in Human Saliva)

  • Song Han
    • Journal of Oral Medicine and Pain
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    • 제20권1호
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    • pp.19-28
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    • 1995
  • 타액은 구강 환경을 조절하는 여러 가지 유기질과 무기질의 혼합물로 구성되어 있다. 구강 점막은 여러 타액 점액 단백질과 타액 항세균 단백질에 의해서 윤활이 되며 보호된다.타액의 다른 작용은 구강 점막을 축축하게 하고 음식을 부드럽게 한다. 구강건조증은 세균의 침착을 야기시키거나 점막면을 거칠게 하여 출혈이 되기 쉽게 하며 이로 인해 감염이 야기될 수 있다. 이러한 타액의 보호 작용은 mucin, fibronectins, proline-rich glycoproteins, histidine-rich proteins, $\alpha$-amylase, s-IgA 같은 특별한 타액 당단백질에 기인한다고 하는 것이 지난 30년 동안에 알려져 있다. 이러한 분자들의 구조, 구조와 기능사이의 관계, 타액 내 이러한 물질들의 농도에 관한 것들이 알려지고 있는 중이다. 이러한 타액 당단백질 특히 mucin, fibronectin, fucose-rich protein과 s-IgA의 구조와 기능에 대한 현재의 견해들을 이 논문에서 요약하고자 한다.

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한국산 밀가루 단백질의 화학적 조성에 관한 연구 (제1보). Gliadin 단백질의 아미노산 조성 및 그의 정제 (Studies on the Chemical Composition of Korean Wheat Flour Proteins (I). Purification of Gliadin Proteins and Amino Acid Composition)

  • 조성희;김준평
    • 대한화학회지
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    • 제21권3호
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    • pp.210-214
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    • 1977
  • 한국산 밀 품종들 중에서 장광의 것을 선정하여 단백질을 추출한 다음 이 단백질의 아미노산 조성과 gliadin 단백질의 정제로 주 gliadin 단백질을 분리하여 본 결과 1. Gliadin과 glutenin 단백질은 다같이 disc 전기이동상에 5개의 band를 나타내었다. 2. Gliadin과 glutenin 단백질은 다같이 glutamic acid의 함량이 가장 많았다. 3. Gliadin과 glutenin 단백질간에 아미노산 조성의 차이는 gliadin이 glutenin보다 alanine의 함량은 적었으나 proline의 함량은 많았다. 4. 주 gliadin 단백질은 gliadin 단백질을 Sephadex G-150과 A-25 coumn으로 정제하여 얻었다.

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