A local renin-angiotensin system in the bone marrow

Haznedaroğlu, İbrahim C.; Tunçer, Serdar; Gürsoy, Murat

doi:10.1016/s0306-9877(96)90122-x

Cited by 64 publications

(56 citation statements)

References 11 publications

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“…1 Presence of a local bone marrow RAS, affecting physiological and neoplastic blood cell production, has been evolved as a novel hypothesis in the past decade. [2][3][4] The forthcoming studies gave countenance to the potent stimulatory affect of angiotensin II in physiological hematopoiesis accordingly in an autocrine-paracrine manner by the findings of increased expression of RAS components such as renin, angiotensinogen and anjiotensin II it-self and its type-1 receptors (AT1R) on hematopoietic stem and precursor cells. 5,6 Angiotensin II stimulates the proliferation of bone marrow hematopoietic progenitors and umbilical cord blood cells.…”

Section: Introductionmentioning

confidence: 99%

Angiotensin Converting Enzyme Insertion/Deletion Gene Polymorphisms in Leukemic Hematopoiesis

Akalın¹

2011

UHOD

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Local bone marrow renin-angiotensin system (RAS) is an autocrine-paracrine system affecting normal and neoplastic hematopoiesis. Angiotensin converting enzyme (ACE) converts angiotensinogen-I to its physiologically active peptide angiotensin-II, which stimulates proliferation and differentiation of hematopoietic stem cells through angiotensin II type 1 receptors. We investigated the ACE insertion/deletion (I/D) gene polymorphisms in patients with hematological malignancies including acute and chronic leukemia, myelodysplastic syndrome and multiple myeloma. Our results showed that 80.4% of the patients represented ID/II genotype, whereas it was 55.9% of the control group and 3.2 fold increased disease risk in the existence of insertion allele (ID/II). This is the first study demonstrating possible effects of ACE I/D gene polymorphism of the local bone marrow RAS components on leukemic hematopoiesis.

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Section: Introductionmentioning

confidence: 99%

Angiotensin Converting Enzyme Insertion/Deletion Gene Polymorphisms in Leukemic Hematopoiesis

Akalın¹

2011

UHOD

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“…30 The autocrine and intracrine functions of the RAS are linked to haematopoiesis regulation by affecting production, proliferation and differentiation of the cells in both normal and malignant haematological processes. 31 The RAS regulates cellular growth in a variety of tissues including the BM and can exert considerable effects on erythropoietic progenitors and primitive pluripotential haematopoietic stem-cell populations. 17 Recent investigations have revealed several RAS elements and receptors on normal and neoplastic haematopoietic cells.…”

Section: Discussionmentioning

confidence: 99%

Elevated serum angiotensin converting enzyme levels as a reflection of bone marrow renin–angiotensin system activation in multiple myeloma

Albayrak

Çelebi

Albayrak

et al. 2012

J Renin Angiotensin Aldosterone Syst

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Introduction: Angiotensin converting enzyme (ACE) is a circulating enzyme that participates in the body's reninangiotensin system (RAS) and is localized on the endothelial cell surface in the lung and other vascular beds. It catalyses the conversion of decapeptide angiotensin I to octapeptide angiotensin II. In the present study, we aimed to analyse the possible relationship between the levels of ACE in the context of RAS in multiple myeloma (MM) pathogenesis. Materials and methods:The study was conducted on 25 MM patients (13 males, 12 females; median age 66 years, range 47-88) and 20 healthy controls. The clinical features of MM patients including demographics and laboratory findings were summarized. Serum ACE levels were measured by using commercially available kits. Results: The serum ACE levels of MM patients and controls were 32.60±20.26 and 15.35±6.47 respectively. Serum ACE levels were significantly higher in MM patients compared with control groups (p<0.001). Conclusions: Being an important component of RAS, circulating ACE might be associated with clonal proliferation of malignant plasma cells in the bone marrow microenvironment. Identification of the pathobiological activity of the local RAS in MM would enlighten the biologic basis and clinical management of haematologic disorders.

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“…In relation to the connective tissue, the RAS is involved the process of myocardial infarction and fibrosis in chronic liver disease 3 . Interestingly, several studies have shown that RAS is involved in bone metabolism 4 . Thus, strategies have been used to decrease the process of bone disorders through RAS inhibition 5 .…”

Section: Introductionmentioning

confidence: 99%

Nandrolone increases angiotensin-I converting enzyme activity in rats tendons

Marqueti

Hashimoto

Durigan

et al. 2015

Rev Bras Med Esporte

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Introduction: The renin-angiotensin system (RAS) has been associated with several biological processes of the human body, regulating, among others blood pressure and water and electrolytes balance. Moreover, RAS also regulates connective tissue growth. Recently, studies have shown that the use of nandrolone modifies the angiotensin-I converting enzyme (ACE) activity and increases collagen deposition in the heart. Objective: The aim of study was to evaluate the Angiotensin-I converting enzyme (ACE) activity in the superficial flexor tendon (SFT) and in serum after load exercise in combination with anabolic androgenic steroid (AAS) administration after training session and six weeks of detraining. Methods: Forty-eight Wistar rats were used into two groups (G1 and G2) subdivided into four subgroups: Sedentary (S); trained (T); AAS-treated (Deca-Durabolin

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A local renin-angiotensin system in the bone marrow

Cited by 64 publications

References 11 publications

Angiotensin Converting Enzyme Insertion/Deletion Gene Polymorphisms in Leukemic Hematopoiesis

Angiotensin Converting Enzyme Insertion/Deletion Gene Polymorphisms in Leukemic Hematopoiesis

Elevated serum angiotensin converting enzyme levels as a reflection of bone marrow renin–angiotensin system activation in multiple myeloma

Nandrolone increases angiotensin-I converting enzyme activity in rats tendons

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