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Biomedical subjects

K S Murthy

Publications and source records attributed to K S Murthy.

At least 19 recordsLinked to original sources
PubMed2006

Development of endosulfan tolerant strain of an egg parasitoid Trichogramma chilonis Ishii (Hymenoptera: Trichogrammatidae).

A strain of T. chilonis, an egg parasitoid of lepidopteran pests tolerant to the most commonly used cyclodiene insecticide--endosulfan was developed in the laboratory. Tolerance to endosulfan was induced by exposing adult parasitoids sequentially from a sub-lethal concentration (0.004%) to the field recommended concentration (0.09%). The strain acquired tolerance to the insecticide after 341 generation of continuous exposure with LC50 values of 1074.96 ppm as compared to LC50 of (70.91 ppm) in susceptible strain. The genetical study showed that F1 crosses exhibited a semi-dominant response to endosulfan with degree of dominance value (D) of 0.58. The resistant factor of tolerant strain was 15.1 folds and of F1 cross were 8.53 folds over susceptible strain. Under net house conditions, the tolerant strain parasitised 56% Helicoverpa armigera eggs on potted cotton plants immediately after an insecticide spray, compared to 3% by the susceptible strain. High percentage survival of the immature stages of the tolerant strain proved their ability to withstand the insecticide load. Breakdown of insecticide tolerance in the strain occurred after four generations in absence of insecticide load. Use of the tolerant strain as a component of bio-intensive IPM in various crops where insecticide use is higher is discussed.

Animals↗
PubMed2001

Activation of phosphodiesterase 5 and inhibition of guanylate cyclase by cGMP-dependent protein kinase in smooth muscle.

The regulation of cGMP-specific phosphodiesterase (PDE) 5 and soluble guanylate cyclase (GC) by cGMP- and cAMP-dependent protein kinases (PKG and PKA respectively) was examined in gastric smooth muscle. The NO donor, sodium nitroprusside (SNP), stimulated PDE5 phosphorylation and activity, which was blocked by the selective PKG inhibitor, KT5823, resulting in an elevation of cGMP levels. Activation of PKA either directly by Sp-5,6-dichloro-1-beta-d-ribofuranosyl benzimidazole 3',5'-cyclic monophosphothioate, or via isoproterenol- and forskolin-dependent increase in cAMP, also caused an increase in PDE5 phosphorylation and activity, but only in the presence of cGMP; consistent with the dependence of PDE5 phosphorylation and activity on cGMP binding to allosteric sites in the regulatory domain of PDE5. The selective PKA inhibitors, myristoylated protein kinase inhibitor and H-89, blocked the increase in PDE5 phosphorylation and activity induced by PKA. SNP also stimulated soluble GC phosphorylation and activity. KT5823 abolished phosphorylation and augmented soluble GC activity, implying feedback inhibition of soluble GC by PKG-dependent phosphorylation. Phosphorylation by PKG was direct and could be induced in vitro. Activation of PKA had no effect on soluble GC. Thus cGMP levels are regulated by PKG- and PKA-dependent activation of PDE5 and PKG-specific inhibition of soluble GC.

3',5'-Cyclic-GMP Phosphodiesterases↗
PubMed2001

A new repair for anomalous left coronary artery.

We report a new technique of left coronary artery implantation to the aorta with interposition of a tube created from the great arterial wall for anomalous left coronary artery from pulmonary artery. This technique was used in 3 patients, of which 2 patients survived. It achieves two coronary artery repair and avoids problems related to extensive mobilization of coronary artery for translocation. It is easily reproducible.

Anastomosis, Surgical↗
PubMed2001

Sequential activation of heterotrimeric and monomeric G proteins mediates PLD activity in smooth muscle.

The identity of G proteins mediating CCK-stimulated phospholipase D (PLD) activity was determined in intestinal smooth muscle cells. CCK-8 activated G(q/11), G(13), and G(12), and the monomeric G proteins Ras-homology protein (RhoA) and ADP ribosylation factor (ARF). Activation of RhoA, but not ARF, was mediated by G(13) and inhibited by Galpha(13) antibody. CCK-stimulated PLD activity was partly mediated by RhoA and could be inhibited to the same extent (47 +/- 2% to 53 +/- 6%) by 1) a dominant negative RhoA mutant, 2) RhoA antibody or Galpha(13) antibody, and 3) Clostridium botulinum C3 exoenzyme. PLD activity was also inhibited by ARF antibody, and the effect was additive to that of RhoA antibody or C3 exoenzyme. PLD activity was inhibited by calphostin C, bisindolylmaleimide I, and a selective protein kinase C (PKC)-alpha inhibitor; the inhibition was additive to that of ARF and RhoA antibodies and C3 exoenzyme. In contrast, activated G(12) was not coupled to RhoA or ARF, and Galpha(12) antibody augmented PLD activity. Thus agonist-stimulated PLD activity is mediated additively by G(13)-dependent RhoA and by ARF and PKC-alpha and is modulated by an inhibitory G(12)-dependent pathway.

ADP Ribose Transferases↗
PubMed2001

Identification of a VIP-specific receptor in guinea pig tenia coli.

Vasoactive intestinal polypeptide (VIP) and pituitary adenylate cyclase-activating peptide (PACAP) interact with VPAC(2) receptors in rabbit and guinea pig (GP) gastric muscle but with functionally distinct VIP and PACAP receptors in GP tenia coli. This study examined whether selectivity for VIP was determined by two residues (40, 41) in the extracellular domain that differ in the VIP receptors of GP gastric and tenial muscle. A mutant rat VPAC(2) receptor (L40F, L41F), and two chimeric receptors in which the NH(2)-terminal domain of rat VPAC(2) receptor was replaced with that of GP gastric (chimeric-G) or tenia coli (chimeric-T) VIP receptors, were constructed and expressed in COS-1 cells. VIP and PACAP bound with equal affinity to wild-type and mutant rat VPAC(2) receptors and to chimeric-G receptor (IC(50): VIP 0.3 +/- 0.1 to 1.5 +/- 0.4 nM, PACAP 0.4 +/- 0.1 to 2.5 +/- 0.1 nM) and stimulated cAMP with equal potency (EC(50): VIP 13 +/- 5 to 48 +/- 8 nM, PACAP 8 +/- 3 to 31 +/- 14 nM). VIP bound with high affinity also to chimeric-T receptor (IC(50): 0.5 +/- 0.1 nM) and stimulated cAMP with high potency (EC(50): 3 +/- 1 nM). In contrast, PACAP exhibited >1,000-fold less affinity for binding or potency for stimulating cAMP. We conclude that GP tenia coli express a VIP-specific receptor and that selectivity is determined by a pair of extracellular phenylalanine residues.

Adenylyl Cyclases↗
PubMed2001

cAMP inhibits IP(3)-dependent Ca(2+) release by preferential activation of cGMP-primed PKG.

The singular effects and interplay of cAMP- and cGMP-dependent protein kinase (PKA and PKG) on Ca(2+) mobilization were examined in dispersed smooth muscle cells. In permeabilized muscle cells, exogenous cAMP and cGMP inhibited inositol 1,4,5-trisphosphate (IP(3))-induced Ca(2+) release and muscle contraction via PKA and PKG, respectively. A combination of cAMP and cGMP caused synergistic inhibition that was exclusively mediated by PKG and attenuated by PKA. In intact muscle cells, low concentrations (10 nM) of isoproterenol and sodium nitroprusside (SNP) inhibited agonist-induced, IP(3)-dependent Ca(2+) release and muscle contraction via PKA and PKG, respectively. A combination of isoproterenol and SNP increased PKA and PKG activities: the increase in PKA activity reflected inhibition of phosphodiesterase 3 activity by cGMP, whereas the increase in PKG activity reflected activation of cGMP-primed PKG by cAMP. Inhibition of Ca(2+) release and muscle contraction by the combination of isoproterenol and SNP was preferentially mediated by PKG. In light of studies showing that PKG phosphorylates the IP(3) receptor in intact and permeabilized muscle cells, whereas PKA phosphorylates the receptor in permeabilized cells only, the results imply that inhibition of IP(3)-induced Ca(2+) release is mediated exclusively by PKG. The effect of PKA on agonist-induced Ca(2+) release probably reflects inhibition of IP(3) formation.

Animals↗
PubMed2000

Coupling of the insulin-like growth factor-I receptor tyrosine kinase to Gi2 in human intestinal smooth muscle: Gbetagamma -dependent mitogen-activated protein kinase activation and growth.

Endogenous insulin-like growth factor-1 (IGF-I) stimulates growth of cultured human intestinal smooth muscle by activating distinct mitogen-activated protein (MAP) kinase-dependent and phosphatidylinositol 3-kinase-dependent signaling pathways. In Rat1 and Balb/c3T3 fibroblasts and in neurons the IGF-I receptor is coupled to an inhibitory G protein, G(i), which mediates G(beta)gamma-dependent MAP kinase activation. The present study determined whether in normal human intestinal smooth muscle cells the IGF-I receptor activates a heterotrimeric G protein and the role of G protein activation in mediating IGF-I-induced growth. IGF-I elicited IGF-I receptor tyrosine phosphorylation, resulting in the specific activation of G(i2). G(beta)gamma subunits selectively mediated IGF-I-dependent MAP kinase activation; G(alpha)i2 subunits selectively mediated IGF-I-dependent inhibition of adenylyl cyclase activity. IGF-I-stimulated MAP kinase activation and growth were inhibited by pertussis toxin, an inhibitor of G(i)/G(o) activation. Cyclic AMP inhibits growth of human intestinal muscle cells. IGF-I inhibited both basal and forskolin-stimulated cAMP levels. This inhibition was attenuated in the presence of pertussis toxin. IGF-I stimulated phosphatidylinositol 3-kinase activation, in contrast to MAP kinase activation, occurred independently of G(i2) activation. These data suggest that IGF-I specifically activates G(i2), resulting in concurrent G(beta)gamma-dependent stimulation of MAP kinase activity and growth, and G(alpha)i2-dependent inhibition of cAMP levels resulting in disinhibition of cAMP-mediated growth suppression.

Adenylate Cyclase Toxin↗
PubMed2000

Heterologous desensitization mediated by G protein-specific binding to caveolin.

We examined the notion that sequestration of G protein subunits by binding to caveolin impedes G protein reassociation and leads to transient, G protein-specific desensitization of response in dispersed smooth muscle cells. Cholecystokinin octapeptide (CCK-8) and substance P (SP) were used to activate G(q/11), cyclopentyl adenosine (CPA) was used to activate G(i3), and acetylcholine (ACh) was used to activate both G(q/11) and G(i3) via m3 and m2 receptors, respectively. CCK-8 and SP increased only Galpha(q/11), and CPA increased only Galpha(i3) in caveolin immunoprecipitates; caveolin and other G proteins were not increased. ACh increased both Galpha(q/11) and Galpha(i3) in a time- and concentration-dependent fashion: only Galpha(q/11) was increased in the presence of an m2 antagonist, and only Galpha(i3) was increased in the presence of an m3 antagonist. To determine whether transient G protein binding to caveolin affected subsequent responses mediated by the same G protein, PLC-beta activity was measured in cells stimulated sequentially with two different agonists that activate either the same or a different G protein. After treatment of the cells with ACh and an m2 antagonist, the phospholipase C-beta (PLC-beta) response to CCK-8 and SP, but not CPA, was decreased; conversely, after treatment of the cells with ACh and an m3 antagonist, the PLC-beta response to CPA, but not CCK-8 or SP, was decreased. Similarly, after treatment with CCK-8 or SP, the PLC-beta response mediated by G(q/11) only was decreased, whereas after treatment with CPA, the PLC-beta response mediated by G(i3) only was decreased. A caveolin-binding Galpha(q/11) fragment blocked the binding of activated Galpha(q/11) but not Galpha(i3) to caveolin-3 and prevented desensitization of the PLC-beta response mediated only by other G(q/11)-coupled receptors. A caveolin-binding Galpha(i3) fragment had the reverse effect. Thus, transient binding of receptor-activated G protein subunits to caveolin impedes reassociation of the heterotrimeric species and leads to desensitization of response mediated by other receptors coupled to the same G protein.

Acetylcholine↗
PubMed2000

Heterologous desensitization of response mediated by selective PKC-dependent phosphorylation of G(i-1) and G(i-2).

This study examined the ability of protein kinase C (PKC) to induce heterologous desensitization by targeting specific G proteins and limiting their ability to transduce signals in smooth muscle. Activation of PKC by pretreatment of intestinal smooth muscle cells with phorbol 12-myristate 13-acetate, cholecystokinin octapeptide, or the phosphatase 1 and phosphatase 2A inhibitor, calyculin A, selectively phosphorylated Galpha(i-1) and Galpha(i-2), but not Galpha(i-3) or Galpha(o), and blocked inhibition of adenylyl cyclase mediated by somatostatin receptors coupled to G(i-1) and opioid receptors coupled to G(i-2), but not by muscarinic M(2) and adenosine A(1) receptors coupled to G(i-3). Phosphorylation of Galpha(i-1) and Galpha(i-2) and blockade of cyclase inhibition were reversed by calphostin C and bisindolylmaleimide, and additively by selective inhibitors of PKCalpha and PKCepsilon. Blockade of inhibition was prevented by downregulation of PKC. Phosphorylation of Galpha-subunits by PKC also affected responses mediated by betagamma-subunits. Pretreatment of muscle cells with cANP-(4-23), a selective agonist of the natriuretic peptide clearance receptor, NPR-C, which activates phospholipase C (PLC)-beta3 via the betagamma-subunits of G(i-1) and G(i-2), inhibited the PLC-beta response to somatostatin and [D-Pen(2,5)]enkephalin. The inhibition was partly reversed by calphostin C. Short-term activation of PKC had no effect on receptor binding or effector enzyme (adenylyl cyclase or PLC-beta) activity. We conclude that selective phosphorylation of Galpha(i-1) and Galpha(i-2) by PKC partly accounts for heterologous desensitization of responses mediated by the alpha- and betagamma-subunits of both G proteins. The desensitization reflects a decrease in reassociation and thus availability of heterotrimeric G proteins.

Adenylyl Cyclase Inhibitors↗
PubMed2000

G(i-1)/G(i-2)-dependent signaling by single-transmembrane natriuretic peptide clearance receptor.

Single-transmembrane natriuretic peptide clearance receptor (NPR-C), which is devoid of a cytoplasmic guanylyl cyclase domain, interacts with pertussis toxin (PTx)-sensitive G proteins to activate endothelial nitric oxide synthase (eNOS) expressed in gastrointestinal smooth muscle cells. We examined the ability of NPR-C to activate other effector enzymes in eNOS-deficient tenia coli smooth muscle cells; these cells expressed NPR-C and NPR-B but not NPR-A. Atrial natriuretic peptide (ANP), the selective NPR-C ligand cANP-(4-23), and vasoactive intestinal peptide (VIP) inhibited (125)I-ANP and (125)I-VIP binding to muscle membranes in a pattern indicating high-affinity binding to NPR-C. Interaction of VIP with NPR-C was confirmed by its ability to inhibit (125)I-ANP binding to membranes of NPR-C-transfected COS-1 cells. In tenia muscle cells, all ligands selectively activated G(i-1) and G(i-2); VIP also activated G(s) via VIP(2) receptors. All ligands stimulated phosphoinositide hydrolysis, which was inhibited by ANP-(1-11), PTx, and antibodies to phospholipase C-beta3 (PLC-beta3) and Gbeta. cANP-(4-23) contracted tenia muscle cells; contraction was blocked by U-73122 and PTx and by antibodies to PLC-beta3 and Gbeta in intact and permeabilized muscle cells, respectively. VIP and ANP contracted muscle cells only after inhibition of cAMP- and cGMP-dependent protein kinases. ANP and cANP-(4-23) inhibited forskolin-stimulated cAMP in a PTx-sensitive fashion. We conclude that NPR-C is coupled to activation of PLC-beta3 via betagamma-subunits of G(i-1) and G(i-2) and to inhibition of adenylyl cyclase via alpha-subunits.

Adenylyl Cyclase Inhibitors↗
PubMed2000

Sustained muscle contraction induced by agonists, growth factors, and Ca(2+) mediated by distinct PKC isozymes.

The role of protein kinase C (PKC) in sustained contraction was examined in intestinal circular and longitudinal muscle cells. Initial contraction induced by agonists (CCK-8 and neuromedin C) was abolished by 1) inhibitors of Ca(2+) mobilization (neomycin and dimethyleicosadienoic acid), 2) calmidazolium, and 3) myosin light chain (MLC) kinase (MLCK) inhibitor KT-5926. In contrast, sustained contraction was not affected by these inhibitors but was abolished by 1) the PKC inhibitors chelerythrine and calphostin C, 2) PKC-epsilon antibody, and 3) a pseudosubstrate PKC-epsilon inhibitor. GDPbetaS abolished both initial and sustained contraction, whereas a Galpha(q/11) antibody inhibited only initial contraction, implying that sustained contraction was dependent on activation of a distinct G protein. Sustained contraction induced by epidermal growth factor was inhibited by calphostin C, PKC-alpha,beta,gamma antibody, and a pseudosubstrate PKC-alpha inhibitor. Ca(2+) (0.4 microM) induced an initial contraction in permeabilized muscle cells that was blocked by calmodulin and MLCK inhibitors and a sustained contraction that was blocked by calphostin C and a PKC-alpha,beta,gamma antibody. Thus initial contraction induced by Ca(2+), agonists, and growth factors is mediated by MLCK, whereas sustained contraction is mediated by specific Ca(2+)-dependent and -independent PKC isozymes. G protein-coupled receptors are linked to PKC activation via distinct G proteins.

Alkaloids↗
PubMed2000

Phorbol-stimulated Ca(2+) mobilization and contraction in dispersed intestinal smooth muscle cells.

This study examined the source of Ca(2+) mobilized by phorbol esters and its requirement for phorbol-induced contraction of smooth muscle cells isolated from the circular and longitudinal layers of guinea pig intestine. Phorbol-12-myristate-13-acetate caused rapid, sustained, concentration-dependent muscle contraction and increase in cystolic free [Ca(2+)](i) in muscle cells from both layers. Maximal contraction was similar to that elicited by receptor-linked agonists, whereas maximal [Ca(2+)](i) was 50% less. The increase in [Ca(2+)](i) was mediated by Ca(2+) release in circular, and Ca(2+) influx in longitudinal muscle cells; only the latter was abolished by methoxyverapamil and in Ca(2+)-free medium. [Ca(2+)](i) was essential for contraction in both cell types: contraction in longitudinal muscle cells was abolished by methoxyverapamil and in Ca(2+)-free medium; contraction in circular muscle cells was abolished only after depletion of Ca(2+) stores. Contraction was abolished by the protein kinase C (PKC) inhibitor calphostin C (1 microM), but was not affected by the myosin light chain kinase inhibitor KT5926 (1 microM), suggesting that activation of myosin light chain kinase was suppressed by phorbol-12-myristate-13-acetate or via PKC. Phorbol-induced contraction of permeabilized circular and longitudinal muscle cells was abolished by pretreatment with a common antibody to Ca(2+)-dependent PKC-alpha,beta,gamma, but was not affected by pretreatment with a specific PKC-epsilon antibody. This study demonstrates the ability of phorbol esters to mobilize Ca(2+) from different sources in different smooth muscle cell types and establishes the requirement of Ca(2+) for phorbol-induced contraction; the latter is exclusively mediated by Ca(2+)-dependent PKC isozymes.

Animals↗
PubMed1999

Identification of the G protein-activating domain of the natriuretic peptide clearance receptor (NPR-C).

We have shown recently that the 37-amino acid intracellular domain of the single-transmembrane, natriuretic peptide clearance receptor, NPR-C, which is devoid of kinase and guanylyl cyclase activities, activates selectively Gi1 and Gi2 in gastric and tenia coli smooth muscle. In this study, we have used synthetic peptide fragments of the N-terminal, C-terminal, and middle regions of the cytoplasmic domain of NPR-C to identify the G protein-activating sequence. A 17-amino acid peptide of the middle region (Arg469-Arg485), denoted Peptide 4, which possesses two N-terminal arginine residues and a C-terminal B-B-X-X-B motif (where B and X are basic and non-basic residues, respectively) bound selectively to Gi1 and Gi2, activated phospholipase C-beta3 via the betagamma subunits, inhibited adenylyl cyclase, and induced smooth muscle contraction, in similar fashion to the selective NPR-C ligand, cANP4-23. A similar sequence (Peptide 3), but with a partial C-terminal motif, had minimal activity. Sequences which possessed either the N-terminal basic residues (Peptide 1) or the C-terminal B-B-X-X-B motif (Peptide 2) were inactive. Peptide 2, however, inhibited G protein activation and cellular responses mediated by the stimulatory Peptide 4 and by cANP4-23, suggesting that the B-B-X-X-B motif mediated binding but not activation of G protein, thus causing Peptide 2 to act as a competitive inhibitor of G protein activation.

Adenylyl Cyclases↗
PubMed1999

Evolving surgical management for ventricular septal defect, pulmonary atresia, and major aortopulmonary collateral arteries.

BACKGROUND: The purpose of this study was to evaluate the results of various surgical modalities that have been evolving for the treatment of ventricular septal defect, pulmonary atresia, and major aortopulmonary collateral arteries. METHODS: From 1993 to May 1997, 14 patients (group 1) were treated with staged unifocalization through thoracotomies and final repair by midsternotomy. From June 1997 to February 1998, 10 patients (group 2) were treated with midsternotomy, single-stage complete unifocalization, and repair. RESULTS: In group 1, 14 patients had 21 procedures (1.5 procedures per patient), of which 3 patients (21%) had final correction. There were two deaths (14%). One patient died of blocked shunt. Another patient who had aneurysmal dilation of homograft tubes that were used for unifocalization died after final repair because of low cardiac output. In group 2, 10 patients had ten surgical procedures for complete unifocalization and 9 of 10 (90%) of them achieved final correction. One patient with low cardiac output in whom we did not close the ventricular septal defect died (10%) of suprasystemic right ventricular pressure. CONCLUSION: In single-stage complete unifocalization, more patients had final correction. It reduces the number of operations and hospitalization and hence is more cost effective than multistaged procedures.

Adolescent↗
PubMed1999

Novel techniques of bidirectional Glenn shunt without cardiopulmonary bypass.

BACKGROUND: We report novel techniques of performing bidirectional Glenn shunt (BDG) without cardiopulmonary bypass (CPB). METHODS: Five cases of single ventricle and pulmonary stenosis (PS) complex were taken up for BDG without CPB. The criteria for case selection were an unrestrictive atrial septal defect (ASD), no atrioventricular (AV) valve regurgitation, and no other intracardiac defects requiring correction. A temporary shunt was established between the superior vena cava (SVC) and contralateral branch pulmonary artery (PA) for venous drainage during SVC clamping for BDG anastomosis in four cases. In case 5, a shunt was put between the SVC and right atrium (RA) for venous drainage, and modified Blalock Taussig shunt and patent ductus arteriosus (PDA) were left open until the completion of the BDG. RESULTS: Central venous pressure (CVP) increased to a mean of 22.4 mm Hg during SVC clamping, with improvement of oxygen (O2) saturation from 62.4% to 82.4%. After Glenn shunt, CVP and O2 saturation maintained at 13.2 mm Hg and 87.4%, respectively. Postoperatively, there were no neurological abnormalities and no hospital mortality. CONCLUSIONS: Our technique provides an excellent venous drainage with improvement of O2 saturation during SVC clamping. It avoids problems related to CPB and economy. It is easily reproducible, with excellent results in a selected group of patients without compromising the completeness of repair.

Adolescent↗
PubMed1999

Role of limited posterior thoracotomy for open-heart surgery in the current era.

BACKGROUND: The earliest open-heart operations were performed employing the thoracotomy approach. Over the years, median sternotomy has become the routine way of approaching the heart. However, lately there has been progressive enthusiasm in minimally invasive techniques for accessing the heart. We present our technique of correction of congenital heart defects employing the limited posterior thoracotomy approach. METHODS: From June 1997 to April 1998, 27 patients underwent correction for various intracardiac defects without any mortality. There were 19 ostium secundum defects, with or without other associated anomalies. There were six sinus venosus defects with partial anomalous pulmonary venous connections. Two patients had perimembranous ventricular septal defects, while 2 patients had partial atrioventricular defects. In 2 other patients, pulmonary stenosis was repaired, using pulmonary valvotomy in 1 patient, whereas the other patient required short transannular patch. RESULTS: The median age was 7 years and the median weight was 20 kg. The median skin-to-skin time was 260 minutes. The median bypass time was 63.25 minutes and the median cross-clamp time was 35.0 minutes. All the patients were extubated within 12 hours following surgery and the median ICU stay was 24 hours. Three patients required blood transfusions in the ICU for significant blood loss and the mean chest drainage was 85 cc per 24 hours. None of the patients had phrenic nerve palsies. None of the patients required additional analgesics other than routine ibuprofen or ketorolac tromethamine. Short-term follow-up revealed no functional or physical disability of the thoracic wall and the right arm. All who underwent surgery with this approach were happy with the limited visibility of their scars. CONCLUSIONS: Limited posterior thoracotomy offers a viable alternative for midsternotomy and submammary thoracotomy. It has the advantage of a scar in the back that does not impede the future growth of the breast tissue and the pectoralis major. Our approach does not need any new instruments and hence no contraptions are necessary to perform the operation with this approach. Our results have shown satisfactory short-term results and better cosmesis.

Adolescent↗