• 제목/요약/키워드: proline-rich

검색결과 89건 처리시간 0.029초

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.

한국인 이하선 타액 내 Proline-rich Protein의 다형현상에 대한 연구 (A Study of Polymorphisms of Proline-Rich Protein in the Korean Population)

  • YS Koo;CY Kim
    • Journal of Oral Medicine and Pain
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    • 제13권1호
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    • pp.35-41
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    • 1988
  • After Akline slab polyacrylamide gel electrophoresis and 3-3' DMB staining of parotid saliva from 100 Korean population, Author have got following conclusions. 1. The gene frequencies of proline-rich protein in the Korean population were Pr1=0.79, Pr2=0.21 2. The gene frequencies of Double-band protein in the Korean population were DB+=0.007, Db-=0.933 3. The gene frequencies of proline-rich protein and Double-band protein of the Korean population were between those of he Chinese and Japanese population.

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한국 울릉도,자월도 거주민의 이하선 타액내 Proline-rich protein(Pr), Double-band protein(Db)과 Salivary acidic protein(Pa)의 유전적 다형 현상에 관한 연구 (A Study of Polymorphisms of Proline-rich Protein, Double-band Protein and Pa Protien in Ullung-do and Jawall-do)

  • Soon-Min Chung;Chong-Youl Kim
    • Journal of Oral Medicine and Pain
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    • 제15권1호
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    • pp.91-104
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    • 1991
  • After alkaline slab polyacrylamide gel electrophoresis and 3.3'-DMB staining of parotid saliva from 48 peoples in Ullung-do and 35 peoples in Jawall-do, the author have got following conclusions. 1. The gene frequencies of Proline-rich protein in Ullung-do were Pr1 =0.719, Pr2=0.281 2. The gene frequencies of Proline-rich protein in Jawall-do were Pr1=0.671, Pr2=0.329 3. The gene frequencies of Double band protein in Ullung-do were Db+=0.087, Db-=0.913 4. The gene frequencies of Double band protein in Jawall-do were Db+=0.0.106, Db-=0.0.894 5. The gene frequencies of Pa protein in Ullung-do were Pa+=0.179, Pa-=0.821 6. The gene frequencies of Pa protein in Jawall-do were Pa+=0.167, Pa-=0.833 7. The gene frequencies of Pr1 of Ullung-do and jawall-do were lower than those of Pr1 in Seoul and Onyang, but similar to those of Pr1 in kangnung and Cheju. 8. The gene frequencies of Db- of Ullung-do and Jawall-do were much higher than those of Db+ in Japanese, Chinese and other populations in Korean.

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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.

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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Proteolytic Activity of Escherichia coli Oligopeptidase B Against Proline-Rich Antimicrobial Peptides

  • Mattiuzzo, Maura;Gobba, Cristian De;Runti, Giulia;Mardirossian, Mario;Bandiera, Antonella;Gennaro, Renato;Scocchi, Marco
    • Journal of Microbiology and Biotechnology
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    • 제24권2호
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    • pp.160-167
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    • 2014
  • Oligopeptidase B (OpdB) is a serine peptidase widespread among bacteria and protozoa that has emerged as a virulence factor despite its function has not yet been precisely established. By using an OpdB-overexpressing Escherichia coli strain, we found that the overexpressed peptidase makes the bacterial cells specifically less susceptible to several proline-rich antimicrobial peptides known to penetrate into the bacterial cytosol, and that its level of activity directly correlates with the degree of resistance. We established that E. coli OpdB can efficiently hydrolyze in vitro cationic antimicrobial peptides up to 30 residues in length, even though they contained several prolines, shortening them to inactive fragments. Two consecutive basic residues are a preferred cleavage site for the peptidase. In the case of a single basic residue, there is no cleavage if proline residues are present in the $P_1$ and $P_2$ positions. These results also indicate that cytosolic peptidases may cause resistance to antimicrobial peptides that have an intracellular mechanism of action, such as the proline-rich peptides, and may contribute to define the substrate specificity of the E. coli OpdB.

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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Novel p104 protein regulates cell proliferation through PI3K inhibition and p27Kip1 expression

  • Han, Seung-Jin;Lee, Jung-Hyun;Choi, Ki-Young;Hong, Seung-Hwan
    • BMB Reports
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    • 제43권3호
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    • pp.199-204
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    • 2010
  • The protein p104 was first isolated as a binding partner of the Src homology domain of phospholipase C$\gamma$1, and has been shown to associate with p85$\alpha$, Grb2. The ectopic expression of p104 reduced cellular growth rate, which was also achieved with the overexpression of only the proline-rich region of p104. The proline-rich region of p104 has been found to inhibit the colony formation of platelet-derived growth factor BB-stimulated NIH3T3 cells and MCF7 cancer cells on soft agar. Mutagenesis analysis showed that the second and third proline-rich regions are essential for growth control, as well as for interaction with p85$\alpha$. Overexpression of p104 increased the level of the cyclin-dependent kinase inhibitor, $p27^{Kip1}$, and inhibited the activity of phosphoinositide 3-kinase (PI3K). In summary, p104 interacts with p85$\alpha$ and is involved in the regulation of $p27^{Kip1}$ expression for the reduction of cellular proliferation.

Structural Study on Apoptosis of Chronic Eosinophilic Leukemia Cells by Interaction of S100A8 with Splicing Factor, Proline and Glutamine-Rich

  • Won, Yubin;Choi, Hyosun;Kim, In Sik;Mun, Ji Young
    • Applied Microscopy
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    • 제47권4호
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    • pp.233-237
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    • 2017
  • Chronic eosinophilic leukemia (CEL) is a myeloproliferative disease with an increased number of mature eosinophils and their precursors, which results in infiltration into organs and organ enlargement. The main cause of this disease is the overexpression of tyrosine kinase. However, there is a need for alternative medication, because some patients are resistant to imatinib, which is a tyrosine kinase inhibitor for leukemia. Many studies have indicated that S100A8 and splicing factor proline and glutamine-rich (SFPQ) function as initiation signals of apoptosis in CEL cells. We reviewed structural studies on CEL cells related to S100A8 and SFPQ. Particularly, this review highlighted microscopic results for the study of S100A8 and SFPQ in CEL cells.