6 research outputs found
μλλ λ λ¦°μ± B-μμ©μ²΄ μκ·Ήμ μν λ¦Όνꡬ λ¨λ°±μ μΈμ°ν
μνκ³Ό/λ°μ¬[μλ¬Έ]
[νκΈ]
λ¨λ°±μ κ°μμ μΈ μΈμ°νκ³Όμ μ΄ μΈν¬μ μ리μ μ΅μ’
λ°μμ 맀κ°νκ±°λ μννλ€κ³ μλ €
μ Έ μλ€. κΈλΌμ΄μ½μ μ ν΄λΉλ°μ λ±μ νμνλ¬Όλμ¬, μΈν¬μ¦μλ°μ, μΈν¬λ§μμμ μ΄μ¨μ΄
λ° λ±μ μ체λ°μ λΏ μλλΌ λ©΄μλ°μκ³μμλ νΉμ λ¨λ°±μ μΈμ°νκ° μ‘°μ μ νλ€κ³ νλ€.
κ°μ’
μ‘°μ§μμ Ξ²μλλ λ λ¦°μ± ν¨κ³Όμ μ½λ¦¬μ νΉμ±μ μ μλ €μ Έ μμΌλ©° νΉν λ¦Όνꡬμ
μ Ξ²μμ©μ²΄μ μνμ¬ λ©΄μ λ° μ체μ νμμ± μ μ§κ° μ‘°μ λλ€κ³ νλ€. Ξ² μλλ λ λ¦°μ±
μμ©μ²΄κ° μκ·Ήλλ©΄ GTP κ²°ν©λ¨λ°±μ ν΅νμ¬ adenylate cyclase νμ±μΌλ‘ cAMPκ° μμ±λκ³ ,
cAMPλ cAMP μμ‘΄μ± kinase (A-kinase)λ₯Ό νμ±νμν¨λ€. νμ±νλ A-kinaseλ λ¨λ°±μ μΈ
μ°ν μν΄μΌλ‘μ¨ μΈμ°νλ¨λ°±μ΄ μ΅μ’
μ μΌλ‘ λ°μμ‘°μ μ κ΄μ¬νλ€κ³ νλ€. κ·Έλ¬λ λ¦Όνꡬμ
μ μ΄λ νΉμ λ¨λ°±μ΄ A-kinaseμ μν΄ νμ±νλμ΄ λ°μμ 맀κ°νλμ§μ λν 체κ³μ μΈ μ°
ꡬλ λμ΄μμ§ μλ€.
λ°λΌμ μ΄λ² μ°κ΅¬μμλ ν°μ₯μ λ¦Όνꡬμμ Ξ²μλλ λ λ¦°μ± μμ©μ²΄ν₯λΆνμ λνλλ
λ¨λ°± μΈμ°ν μμμ κ΄μ°°νκ³ , μ€κ°κ³Όμ μ μ κ²νμ¬ Ξ²μμ©μ²΄μκ·Ήνμ A-kinaseμ μνμ¬
μΈμ°νλλ νΉμ΄ κΈ°μ§λ¨λ°±μ μ°Ύκ³ μ νμλ€.
μ€ν μ¬λ£λ‘λ ν°μ₯(Sprague-Dawley)μ λλ§₯νμ λ¦Όνꡬλ₯Ό μ΄μ©νμκ³ , Ξ²μμ©μ²΄ν₯λΆν
λ°μμ μΆνκΉμ§μ μ€κ°λ¨κ³λ₯Ό μΆκ΅¬νκΈ° μνμ¬ isoproterenol, propranolol, forskolin
, cAMP λ° H-8μ μ¬μ©νμλ€.
λΆλ¦¬λ λ¦Όνꡬλ₯Ό [(32)**P ] orthophosphateλ‘ νμ§μν¨ ν λ¦Όνꡬλ₯Ό κ· μ§νν ν μμ¬
λΆλ¦¬νμ¬ λ¨λ°±λΆνμ μ»κ³ , μ΄λ₯Ό NEPHGEμ SDS-PAGEλ₯Ό μ΄μ©ν μ΄μ°¨μμ κΈ°μλλ²μ μ΄μ©ν
μ¬ λ¨λ°±μ λΆλ¦¬ν ν 건쑰μν¨ gelμ μκ°λ°©μ¬κΈ°λ‘λ²μΌλ‘ μΈμ°νλ¨λ°±μ κ΄μ°°νμλ€. ννΈ
λ¦Όνꡬλ₯Ό 미리 κ· μ§νμμΌ λ§λ κ° μΈν¬λΆνμμλ μ½λ¬Όμ²λ¦¬ν [Ξ³-(32)**P ]ATPλ‘ μΈμ°
νμν¨ ν λμΌν λ°©λ²μΌλ‘ μΈμ°ν λ¨λ°±μ κ΄μ°°ν¨μΌλ‘μ¨ μμμ μ»μ΄μ§ μΈμ°νλ¨λ°±μ΄ μΈ
ν¬μ μ΄λ λΆνμ μμΉνλκ°λ₯Ό νμΈνμλ€.
μ€νκ²°κ³Όλ λ€μκ³Ό κ°λ€.
1. Isoproterenol (10**-5 M)μ ν°μ₯ λ¦Όνκ΅¬μΈ μ¬λ¬ λ¨λ°±μ μΈμ°ν νμμΌλ©°, κ·Έμ€ λΆ
μλ 44kD λ±μ μμ 6.3(44kD/6.3) λ¨λ°±μ μΈμ°νκ° λνλ¬λ€.
2. λ¦Όνꡬμ 44kD/6.3 λ¨λ°±μ μΈμ°νλ propranolol 10**-5 M μ μ²μΉμ μνμ¬ μ΅μ λ
μλ€.
3. 44kD/6.3λ¨λ°±μ forskolinμ μνμ¬ λλμμ‘΄μ μΌλ‘ μΈμ°νμ λκ° μ¦κ°νμλ€.
4. λ¦Όνꡬ κ· μ§μ‘μ μΈν¬λ§ λΆνμ cAMPλ₯Ό 첨κ°νμμ λ 44kD/6.3 λ¨λ°±μ μΈμ°νκ° μ
λ°λμλ€.
5. 44kD/6.3 λ¨λ°±μ μΈμ°νλ A-kinase μ΅μ μ¬μΈ H-8μ μνμ¬ μΈμ°νκ° μ΅μ λμλ€.
6. 44kD/6.3 λ¨λ°±μ μΈν¬λ§ λΆνμμλ κ΄μ°°λμμΌλ, μΈν¬μ§λΆνμμλ κ΄μ°°λμ§ μμ
λ€.
μ΄μμ μ€νκ²°κ³Όλ‘ λ³΄μ ν°μ₯ λ¦Όνꡬ λ¨λ°±μ€ λΆμλ 44kD, λ±μ μμ 6.3μ λ¨λ°±μ Ξ²μ
μ©μ²΄ μκ·Ή, adenylate cyclase νμ±ν, cAMP μμ± λ° A-kinase νμ±νμ μνμ¬ μΈμ°νλ
λ λ¨λ°±μμ μ μ μμμΌλ©°. μ΄ λ¨λ°±μ μΈμ°νκ° Ξ²μμ©μ²΄μκ·Ήμ μν λ¦Όνꡬ κΈ°λ₯λ³λ
μ κ΄μ¬ν κ²μΌλ‘ μΆμΈ‘λλ€.
Protein Phosphorylation in Murine Peripheral Lymphocytes by Ξ² Adrenoceptor
Stimulation
De Yeun Oh
Deparment of Medical Science The Graduate School, Yonsei University
(Directed by Associate Prof, Young Soo Ahn. M.D.)
Reversible protein phosphorylation has been known as an important biological
mechanism of cellular regulation such as carbohydrate metabolism, cell
proliferation, ion transport through cell membrane and also in immunologic system.
Beta adrenergic stimulation causes activation of adenylate cyclase and subsequent
accumulation of intracellular cyclic adenosine monophosphate (cAMP) and activation
of cAMP-dependent protein kinase (A-kinase). Lymphocytes possess Ξ² adrenoceptors
on their plasma membranes and stimulation of Ξ² adrenoceptor causes inhibition of
antibody production, lymphocyte proliferation and T cell mediated cytolysis.
Specific substrate protein for A-kinase is thought to be a final mediator for those
cellular responses.
In this study, therefore, it was attempted to characterize the substrate protein
for the A-kinase after Ξ² receptor stimulation in murine peripheral lymphocytes,
Rat peripheral lymphocytes were isolated by centrifugation with Histopaque and
incubated with isoproterenol, propranolol, forskolin, cAMP or H-8.
Proteins were labelled with [(32)**P ] orthophosphate for the intact lymphocyte
or [Ξ³-(32)**P ] ATP for the lymphocyte homogenate. The proteins were separated by
means of two dimensional gel electrophoresis using non-equilibrium pH gradient
electrophoresis and sodium dodecyl sulphate-polyacrylamide gel electrophoresis.
Gels were dried and phosphorylated proteins were observed by autoradiogrhphy.
Results obtained were as follows;
1. Beta adrenergic stimulation of the lymphocyte with isoproterenol (10**-5M )
caused intense phosphorylation of a protein having 44 kD mol wt. and pl 6.3 (44
kD/6.3) which was not observed in the absence of isoproterenol stimulation.
2. Phosphorylation of 44kD/6.3 protein induced by isoproterenol was inhibited by
the pretreatment with propranolol (10**-5M ).
3. Activation of adenylate cyclase by forskolin caused a phospherylation of the
44 kD/6.3 protein dose-dependently,
4. The 44 kD/6.3 protein was phosphorylated by the addition of cAMP in the
lymphocyte homogenate,
5. The phosphorylation of the 44 kD/6.3 protein was selectively inhibited by H-8.
6. The 44 kD/6.3 protein was present in lymphocyte membrane fraction but not in
cytosolic fraction.
These results suggest that the 44 kD/6.3 protein may be the substrate protein
phosphorylated by Ξ²-adrenergic stimulation and the phosphorylation of this protein
would be related to the functional changes in rat lymphocytes by Ξ²-adrenergic
stimulation.restrictio
ꡬμμ CT26 μ μ λͺ¨λΈμμ μ’ μμ μ§νμ λ°λ₯Έ λ©΄μμ§νμ λ³ν
νμλ
Όλ¬Έ(λ°μ¬)--μμΈλνκ΅ λνμ :μνκ³Ό λ΄κ³Όνμ 곡,2005.Docto
μ μλ MALTν λ¦Όνμ’ μ μ μΈν μλ°μ± μμ₯κ΄ λ¦Όνμ’ μμ μ΄μΉλ£λ‘ μ¬μ©λ νμννμλ²μ ν¨κ³Ό
Thesis (master`s)--μμΈλνκ΅ λνμ :μνκ³Ό λ΄κ³Όνμ 곡,2002.Maste
Motor Berve Conduction Velocity in Untreated Maturity-Onset Diabetes
μνκ³Ό/μμ¬[μλ¬Έ]
[νκΈ]
μ κ²½μ‘°μ§μ ν¬λλΉμ μΈν¬λ΄ ν¬κ³Όμ μΈμλ¦°μ νμλ‘ νμ§ μμΌλ©° λ°λΌμ κ³ νλΉμ΄ μ§
μλ κ²½μ° μ κ²½μΈν¬λ΄μ ν¬λλΉ λ° κ·Έ λμ¬μ°λ¬Ό λλκ° λμμ Έμ μ κ²½μΈν¬μ ν΄νμ± λ³ν
κ° μ΄λλλ€.
λ³Έ μ°κ΅¬μμλ λΉλ¨λ³νμμμ κ³ νλΉμ΄ μ κ²½λ³λ³μ λ―ΈμΉλ μν₯μ κ΄μ°°νκΈ° μνμ¬ 30
μμ λΉλ¨λ³νμ λ° 15μμ μ μλμ‘°κ΅°μμ μ΄λμ κ²½μ λμλλ₯Ό μΈ‘μ νμ¬ λ€μκ³Ό κ°μ κ²°
κ³Όλ₯Ό μ»μλ€.
1. λΉλ¨λ³νμμ μ΄λμ κ²½μ λμλλ μ μμΈμ λΉν΄ μμμκ² κ°μλμλ€.
2. λΉλ¨λ³νμμμ μ΄λμ κ²½μ λμλλ 곡볡μ νλΉλκ³Ό μλΉλ‘ κ΄κ³λ₯Ό λνλ΄μλ€.
3. λΉλ¨λ³νμμμ μ΄λμ κ²½μ λμλμ λΉννμμ μ¬μ΄μλ μ μν μκ΄κ΄κ³κ° μμλ€
.
4. νμμ μ°λ Ή λ° λΉλ¨λ³ μ΄νκΈ°κ°κ³Ό μ΄λμ κ²½μ λμλ μ¬μ΄μλ μ μν μκ΄κ΄κ³κ°
μμλ€.
μ΄μμ μ±μ μΌλ‘ 보μ λΉλ¨λ³μ± λ° λ§μ΄μ κ²½μΌμ νλΉκ³Ό λ°μ ν κ΄κ³λ₯Ό κ°μ§κ³ μλ€κ³
보며 νλΉμΉμ μ§μμ μΈ μ‘°μ λ‘ μ κ²½κΈ°λ₯μ 보쑴 λ΄μ§ νΈμ μν¬ μ μλ€κ³ μκ°λλ€.
Motor Nerve Conduction Velocity in Untreated Maturity-Onset Diabetes
Do Yeun Oh
Department of Medical Science The Graduate School Yonsei University
(Directed by Prof. Kyung Hwan Kim, M.D.)
Peripheral neuropathy is a frequent and often disabling complication of diabetes
mellitus. Abnormalities of neural function in diabetes, such as slowed nerve
conduction, may be related to the metabolic derangement in this disease, but the
role of metabolic abnormalities in the development of diabetic neuropathy is
controversial. To investigate the influence of hyperglycemia on nerve concution,
conduction velocities of median, peroneal and tibial nerve were measured in 30
untreated maturity-onset diabetic patients and 15 normal control subjects.
The results are as follows;
1. The motor nerve conduction velocities of median, peroneal, and tibial nerves
were significantly slower in diabetics than normal.
2. Motor conduction velocity was inversely correlated with levels of fasting
plasma glucose in diabetics.
3. Levels of glycosylated hemoglobin, an index of long-term glycemia, were not
correlated with motor nerve conduction velocity.
4. Age and duration of diabetes were not related to the motor nerve conduction
velocity.
Theae findings suggest that the degree of hyperglycemia contributes to the
slowing of motor nerve conduction velocity in untreated maturity-onset diabetes,
but further studies are needed to clarify the relation with glycosylated hemoglobin
and nerve conduction velocity diabetes.restrictio
μ μ μ¬μ±μ μ λ°©μ λ°μν μλ°μ± νλ§ μ‘μ’ 1μ
νλ§ μ‘μ’
μ μ£Όλ‘ κ΄μ μ£Όμ μ‘°μ§μ νΈλ°νλ μ
μ± μ’
μμ΄λ€. μ’
μ’
κ΄μ μ΄μΈμ λ€λ₯Έ λΆμμ λ°μνλ κ²½μ°λ λ³΄κ³ λμ΄μλλ°, μλ°μ± μ λ°© νλ§ μ‘μ’
μ μΈκ³μ μΌλ‘λ λ³΄κ³ λ μκ° λλ¬Όλ€. λ³Έ μ¦λ‘λ μλ°μ± μ λ°© νλ§ μ‘μ’
μΌλ‘ μ§λ¨λ 15μΈ μ¬μ νμμ 1μμ΄λ€. μ§λ¨ ν μ λ°© μ’
κ΄΄μ λν κ΄λ²μ μ μ μ μ μννμμΌλ 9κ°μ ν κ΅μ μ¬λ°νμκ³ , μ΄μ μ¬λ° λΆμμ λν κ΄λ²μ μ μ μ μ λ€μ μννμλ€. κ·Έλ¬λ, 27κ°μ ν νμ μ°μμ½μ κ³ λ¦½μ± ν μ μ΄κ° λ°κ²¬λμλ€. μ΄μ ν λ³λ³μ λν μ μ μ λ° κ³ μμ ννμλ²μΌλ‘ doxorubicin λ° ifosfamideμ λ³ν© ννμλ²μ μννμλ€. νμ¬ νμννμλ² μ’
λ£ ν 28κ°μμ§Έ μ¬λ°μ μ¦κ±° μμ΄ κ²½κ³Όκ΄μ°° μ€μ΄λ€. μ΄μ μ μλ€μ λ³Έ μ¦λ‘λ₯Ό λ¬Ένκ³ μ°°κ³Ό ν¨κ» λ³΄κ³ νλ λ°μ΄λ€
The Impact of Primary Tumor Resection on the Survival of Patients with Stage IV Breast Cancer
Purpose The main treatment for stage IV breast cancer is currently systemic therapy. Surgical resection of the primary tumor is usually done for treating the tumor-related complications Recent studies have suggested that surgery may improve the long-term survival of stage IV breast cancer patients We evaluated the impact of the primary surgical resection site on the survival of stage IV breast cancer patients. Methods We reviewed the records of the stage IV breast cancer patients who were treated at Seoul University Hospital between April 1992 and December 2007 The tumor and clinical characteristics, the type of treatments and the overall survival were compared between the surgically versus nonsurgically treated patients. Results. Of the 198 identified patients, 110 (55 8%) received surgical excision of their primary tumor and 88 (44 2%) did not The mean survival was 67 months vs. 42 months for the surgically treated patients vs the patients without surgery, respectively (p=0 0287) On a multivariate analysis with using the Cox model and after adjusting for the estrogen receptor status, visceral metastases, the number of metastatic sites and trastuzumab treatment, surgery was an independent factor for improved survival (hazard ratio, 0.55; 95% confidence interval, 0.31-0.97; p=0.041). Conclusion Surgical resection of the primary tumor in stage IV breast cancer patients was independently associated with improved survival. Randomized prospective trials are needed to firmly recommend surgical resection of the primary tumor in stage IV breast cancer patientsλ³Έ μ°κ΅¬λ νμ, μ λ°©μ/λμμ μ μ 체 μ°κ΅¬μΌν°μ μ°κ΅¬λΉλ₯Ό μ§μλ°μ μν
λμμ(01-PJ3-PG6-01GN07-0004).Bafford AC, 2009, BREAST CANCER RES TR, V115, P7, DOI 10.1007/s10549-008-0101-7Blanchard DK, 2008, ANN SURG, V247, P732, DOI 10.1097/SLA.0b013e3181656d32*KOR BREAST CANC S, 2008, BREAST CANC FACTS FI, V1, P5Fields RC, 2007, ANN SURG ONCOL, V14, P3345, DOI 10.1245/s10434-007-9527-0Gnerlich J, 2007, ANN SURG ONCOL, V14, P2187, DOI 10.1245/s10434-007-9438-0Rapiti E, 2006, J CLIN ONCOL, V24, P2743, DOI 10.1200/JCO.2005.04.2226Morrow M, 2006, J CLIN ONCOL, V24, P2694, DOI 10.1200/JCO.2006.05.9824Babiera GV, 2006, ANN SURG ONCOL, V13, P776, DOI 10.1245/ASO.2006.03.033Hotta T, 2006, ANTICANCER RES, V26, P1377Abe O, 2005, LANCET, V366, P2087Andre F, 2004, J CLIN ONCOL, V22, P3302, DOI 10.1200/JCO.2004.08.095Giordano SH, 2004, CANCER, V100, P44, DOI 10.1002/cncr.11859Khan SA, 2002, SURGERY, V132, P620, DOI 10.1067/msy.2002.127544Flanigan RC, 2001, NEW ENGL J MED, V345, P1655Demicheli R, 2001, BRIT J CANCER, V85, P490Dauplat J, 2000, SEMIN SURG ONCOL, V19, P42Overgaard M, 1999, SEMIN RADIAT ONCOL, V9, P292DOGHETTO GB, 1999, AM SURGEON, V65, P352BLAND KI, 1998, BREAST COMPREHENSIVE, V2Ragaz J, 1997, NEW ENGL J MED, V337, P956OREILLY MS, 1994, CELL, V79, P315FISHER B, 1989, CANCER RES, V49, P1996*NAT CANC I, BREAST CANC TREATM P