• 제목/요약/키워드: secretory protein

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

  • San Kim;Chang-Lyuk Yoon
    • Journal of Oral Medicine and Pain
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    • v.19 no.2
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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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Effect of Adrenergic Nervous System on Pancreatic Exocrine Secretion in Rats (흰쥐에서 췌장의 외분비 기능에 미치는 adrenaline 동작성 신경계의 영향)

  • Shin, Won-Im;Kim, Mi-Ryoung;Kwon, Hyeok-Yil;Lee, Yun-Lyul;Park, Hyoung-Jin
    • The Korean Journal of Physiology
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    • v.20 no.2
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    • pp.249-256
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    • 1986
  • The present study was performed to investigate a possible influence of the adrenergic nervous system on pancreatic exocrine secretion stimulated by intraduodenal acid perfusion. Pancreatic secretion was collected in rats anesthetized with urethane after 24 hours fasting. The duodenal lumen was perfused (0.2 ml/min) with HCI solution in a concentration of 0.005, 0.01, 0.02, 0.05 or 0.1 N When the volume of panceratic juice secreted for IS min became constant phentolamine (1 mg/kg), $noradrenaline\;(10\;{\mu}g/kg),\;Propranolol\;(1\;mg/kg),\;and \;isoproterenol\;(1\;{\mu}g/kg)$ were administered through the jugular vein in bolus. The secretory volume and protein output were measured in the pancreatic juice collected for 15 min. 1) HCI, perfused intraduodenally in graded concentrations from 0.005 N to 0.1 N, increased the pancreatic secretory volume and protein output dose-dependently. 2) In the basal state as well as in the stimulated state by the duodenal acid perfusion, phentolamine increased the pancreatic secretory volume and protein output while propranolol inhibited the volume and protein output. 3) In the basal state, noradrenaline did not change the pancreatic secretory volume but increased the protein output while isoproterenol increased both of the secretory volume and the protein output. These results strongly suggest that ${\alpha}-adrenoceptors$ in the rat pancreas exert an inhibitory influence on the pancreatic exocrine secretion including volume and protein output in the basal state as well as in the stimulated state by the intraduodenal acid perfusion while ${\beta}-adrenoceptors$ play a stimulatory role in the pancreatic exocrine secretion. However, in the physiological situation, adrenergic excitation may stimulate the protein output through ${\beta}-adrenoceptors$ without change in the secretory volume in the rat pancreas.

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Comprehensive Proteome Analysis of the Excretory/Secretory Proteins of Toxoplasma gondii

  • Lee, Won-Kyu;Ahn, Hye-Jin;Baek, Je-Hyun;Lee, Chong-Heon;Yu, Yeon Gyu;Nam, Ho-Woo
    • Bulletin of the Korean Chemical Society
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    • v.35 no.10
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    • pp.3071-3076
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    • 2014
  • Proteomic analyses of the excretory/secretory proteins from the RH strain of Toxoplasma gondii have been performed to understand their functions in the host-parasite interaction. A total of 34 proteins were identified from LC/MS/MS analysis and their abundance was estimated by spectral counting methods. Among them, 8 species of micronemal proteins (MICs), 2 species of rhoptry proteins (ROPs), and 6 species of dense granular proteins (GRAs) were confirmed. Besides these, 18 species of protein were newly identified, and their cellular functions were estimated from sequence analysis. The three most abundant of the 34 identified extractor/secretory proteins-GRA1, GRA7 and GRA2-were confirmed to be highly expressed in T. gondii using the spectral count method. This phenomenon is another demonstration of the importance of GRA proteins for the penetration and survival of T. gondii.

Emerging Mechanisms of Cyr61/CTGF/NOV Secretion in the Nervous System

  • Yang, Hayoung;Park, Young-Jun;Shim, Sungbo
    • Biomedical Science Letters
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    • v.28 no.2
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    • pp.59-66
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    • 2022
  • The Cyr61/CTGF/NOV (CCN) family is dynamically expressed in various tissues, including the nervous system, from the prenatal period to adulthood. However, major studies have been conducted only in limited fields, such as the cardiovascular and muscular systems, skeletal development, and cancer. In addition, although the CCN family is a secretory protein, very few studies have described its mechanism of secretion. Recently, it has been suggested that overexpression of CCN3 or intracellular accumulation due to problems in the secretory pathway can inhibit neuronal axonal growth. In this review, we have briefly summarized the structure and characteristics of the CCN family and its related diseases, with particular emphasis on the secretory mechanism and modifiers of the CCN family, newly identified in the nervous system.

Fine Structural Analysis of Secretory Silk Production in the Black Widow Spider, Latrodectus mactans

  • Mun, Myeong-Jin;Mark A. Townley;Edward K. Tillinghast
    • Animal cells and systems
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    • v.2 no.1
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    • pp.145-152
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    • 1998
  • The spinning apparatus and production of secretory silk from silk gland of the black widow spider, Latrodectus mactans were studied with scanning and transmission electron microscopes. The silk glands were located in seven groups on the spinnerets including each pair of major and minor ampullate, 3 pairs of tubuliform, 1 pair of flagelliform, 2 pairs of aggregate, about 50 pairs of pyriform and over 250 pairs of aciniform glands, respect- ively. Each group of silk gland feeds silk into one of the three spinneret pairs. Secretory silk is synthesized from rough endoplasmic reticulum (rER) of glandular epithelial cells. The secretory silk is transported from toe rER into the secretory vacuoles which are grown up by fusion with the surrounding small vesicles including the secretory silk. The secretory vacuoles, which show a gradual increase in electron density with the process of maturity, are formed without involvement of the Golgi complex, suggesting that they do not play an important role in the processing of the secretory silk. The secretory silk products are released by the mechanism of apocrine secretion, losing part of their cytoplasm. Moreover, another type of silk precursor, possibly protein, appears as granular material, and is also discharged to the luminal cavity.

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The predictive value of serum myeloma protein in solitary plasmacytoma

  • Chang, Won Ick;Koh, Hyeon Kang;Yoon, Sung-Soo;Kim, Han-Soo;Eom, Keun-Yong;Kim, Il Han
    • Radiation Oncology Journal
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    • v.38 no.2
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    • pp.129-137
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    • 2020
  • Purpose: To identify the clinical usefulness of serum M protein and to establish a rationale for regular follow-up with serum protein electrophoresis in solitary plasmacytoma. Materials and Methods: Sixty-nine patients with solitary plasmacytoma and solitary plasmacytoma with minimal marrow involvement according to the International Myeloma Working Group criteria were retrospectively reviewed. Results: At a median follow-up of 6.2 years, 5-year local control (LC), 5-year multiple myeloma-free survival (MMFS), 5-year failure-free survival (FFS), and 5-year overall survival (OS) were 82.6%, 44.1%, 41.8%, and 85.1%, respectively. Among the patients whose initial serum M protein was present or not evaluated, 37.3% of patients showed disappearance of serum M protein after various treatment. MMFS of these patients were comparable to non-secretory plasmacytoma with undetectable levels of M protein, and significantly better than patients with persistent M protein. Increase of serum M protein ≥0.1 g/dL was most predictive of treatment failure with area under the curve of 0.731. Conclusion: Patients who eventually showed persistence of serum M protein after treatment showed worse MMFS and FFS compared to those whose serum M protein disappeared or who had initially non-secretory disease. The increase of serum M protein level ≥0.1 g/dL from current nadir was predictive of treatment failure. Therefore, regular follow-up with serum M protein is highly recommended especially unless the patient had initially non-secretory disease.

Intensive Proteomic Approach to Identify Secreted Peptides/Proteins from 3T3-L1 Adipocytes using Gel Electrophoresis and Liquid Chromatograph Separation Methods (젤 전기영동 및 액체 크로마토그래피 분리 방법을 이용하여 지방 세포로부터 분비되는 단백질들에 대한 프로테오믹스 연구 방법)

  • Hwang, Hyun-Ho;Baek, Moon-Chang
    • YAKHAK HOEJI
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    • v.55 no.3
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    • pp.203-212
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    • 2011
  • Adipocytes have been known to secrete a number of important proteins called adipokines with roles in energy metabolism, reproduction, cardiovascular function and immunity. In this study we have attempted to identify intensively secretory proteins from 3T3-L1 adipocytes. 3T3-L1 preadipocytes were differentiated into mature adipocytes and then the cells were left in serum-free medium. The supernatant was filtrated and dialyzed. Lyophilized secretome was fractionated by two different methods, 1-D SDS PAGE and RP-FPLC. The tryptic peptides from the gel slices and the FPLC fractions were analyzed by nanoLC/ESI-MS/MS. We identified a total of 303 identical proteins from two methods, 251 proteins from 1-D gel and 184 proteins from RP-FPLC. 86 of them were listed as a secretory protein Finally, we identified many known or unknown secreted proteins existed in the low level including adiponectin, angiotensinogen, bone morphogenetic protein-1 (BMP-1), macrophage migration inhibitory factor (MIF), insulin like growth factor-II (IGF-II), interleukin-6 (IL-6), follistatin-related protein-1, minecan, and resistin. The existence of some of secreted proteins has been confirmed in RNA level. This proteomic experiment is useful for the intensive screening of secretory proteins in many kinds of other cells.

The Change of Secretory Activity of the Alveolar Type ll Cell During Acute Alveolar Injury Induced by N-Nitroso-N-Methylurethane

  • Lee, Young-Man;Bang, In-Sook;Lee, Suck-Kang
    • The Korean Journal of Physiology
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    • v.28 no.1
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    • pp.71-77
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    • 1994
  • In the animal model of acute respiratory distress syndrome (ARDS) induced by N-nitroso-N-methylurethane (NNNMU) the secretory activity of alveolar type H cells during acute alveolar injury was investigated by determining phospholipid and pulmonary surfactant associated proteins in crude surfactant. The mechanism of the secretory change was studied by determination of DNA and RNA levels in the lung tissue. After induction of acute alveolar injury with NNNMU, pulmonary hemorrhage, atelectasis and gross hypertrophy were observed. Seven days after NNNMU treatment the level of total DNA in lung homogenate was increased markedly indicating that a hypertrophy was induced by cellular proliferation. Although the total DNA level increased, the RNA/DNA ratio was gradually decreased after NNNMU treatment. Seven days after NNNMU treatment the RNA/DNA ratio returned to the normal control level. During the acute alveolar injury, phospholipid and surfactant associated proteins were reduced significantly as compared with the control, implying that the secretory activity of alveolar type II cells was altered during acute alveolar injury induced by NNNMU. The protein content in crude surfactant during peak injury(7 days after NNNMU) was decreased significantly but phospholipid/protein ratios were identical in both control and NNNMU treatment groups. SDS-PAGE of proteins in crude pulmonary surfactant showed a decrease in major surfactant associated protein(M.W. 38,000) during acute alveolar injury. The present study may suggest that while alveolar type H cells proliferate markedly, transcription of alveolar type ll cell gene was inhibited by an unknown mechanism such as DNA methylation induced by NNNMU. Such an inhibition of transcriptional activity is thought to be associated with the decreased secretory activity of alveolar type ll cells, which may lead to pulmonary atelectasis and edema during the acute alveolar injury.

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Effect of Prunus mume extract(PME)-containing chewing gum mastication on the change of saliva ingredients

  • Jang, Jong-Hwa;Lee, Young-Soo
    • Journal of Korean society of Dental Hygiene
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    • v.16 no.3
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    • pp.463-469
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    • 2016
  • Objectives: The purpose of the study is to investigate the effect of chewing gum containing Prunus mume extract(PME) on the change of saliva ingredients. On the basis of the biological background of molecules and diagnostic indices in the use of saliva, the mastication effect of chewing gum containing PME was demonstrated in terms of secretory IgA concentration and total protein concentration in stimulated saliva. Methods: This study is an experimental research on the use of a research design before and after applying a randomized control group. Participants were distributed randomly to the experimental group and the control group, respectively. The experiment group was instructed to masticate the chewing gum containing PME for 10 minutes for one month after each meal within 30 minutes. Salivary secretion was collected by the participants between 8 and 10 a.m in the morning in the research office. For the measurement of secretory IgA and total protein concentrations in the saliva, indirect enzyme-linked immunosorbent assay(ELISA) was used. Results: The salivation stimulation rate was significantly increased after four weeks of masticating chewing gum containing PME after each meal(p<0.001). Mastication of chewing gum containing PME for four weeks decreased the concentration of secretory IgA much more significantly than that after mastication for one week(p=0.003). The concentration of total protein in the saliva was decreased after four weeks in the experimental and control groups. Conclusions: Mastication of chewing gum containing PME stimulated salivary secretion and led to oral disease prevention in patients with xerostomia. Furthermore, it seems to be urgent to seek measures that can be utilized in intervention for patients with xerostomia.

Induction of a systemic IgG and secretory IgA responses in mice by peroral immunization with uropathogenic Escherichia coli adhesin protein coupled to cholera toxin A2B subunits

  • Lee, Yong-Hwa;Kim, Byung-Oh;Rhee, Dong-Kwon;Pyo, Suh-Kneung
    • Biomolecules & Therapeutics
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    • v.11 no.3
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    • pp.157-162
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    • 2003
  • The generation of secretory IgA antibodies(Abs) for specific immune protection of mucosal surfaces depends on stimulation of the mucosal immune system, but this is not effectively achieved by parenteral or even oral administration of most soluble antigens. Thus, to produce a possible vaccine antigen against urinary tract infections, the uropathogenic E. coli (UPEC) adhesin was genetically coupled to the ctxa2b gene and cloned into a pMAL-p2E expression vector. The chimeric construction of pMALfimHIctxa2b was then transformed into E. coli K-12 TB1 and its nucleotide sequence was verified. The chimeric protein was then purified by applying the affinity chromatography. The purified chimeric protein was confirmed by SDS-PAGE and western blotting using antibodies to the maltose binding protein (MBP) or the cholera toxin subunit B (CTXB), plus the N-terminal amino acid sequence was analyzed. The orderly-assembled chimeric protein was confirmed by a modified $G_{M1}$-ganglioside ELISA using antibodies to adhesin. The results indicate that the purified chimeric protein was an Adhesin/CTXA2B protein containing UPEC adhesin and the $G_{M1}$-ganglioside binding activity of CTXB. This study also demonstrate that peroral administration of this chimeric immunogen in mice elicited high level of secretory IgA and serum IgG Abs to the UPEC adhesin. The results suggest that the genetically linked CTXA2B acts as a useful mucosal adjuvant, and that the adhesin/CTXA2B chimeric protein might be a potential antigen for oral immunization against UPEC.