The Renin-Angiotensin System in the Endocrine

Department of Medical Cell Biology, Uppsala University. Uppsala, Sweden
Experimental data suggest that a tissue renin-
angiotensin system is present in the pancreatic
islets of several species, including man.
However, the physiological role for this local
renin-angiotensin system remains largely
unknown. In vitro findings argue against a
direct effect of angiotensin II on alpha- and
beta-cells. In contrast, when the influence of
angiotensin II on the pancreatic islets has
been evaluated in the presence of an intact
vascular system either in vivo or in the
perfused pancreas, a suppression of insulin
release has been observed, also in man. These
discrepancies may be explained by the
profound effects of the renin-angiotensin
system on pancreatic islet blood perfusion.
Alterations in the systemic renin-angiotensin
system and an increased vascular sensitivity
for its components have been observed in
diabetes mellitus and hypertension.
Whether changes occur also in the pancreatic
islet renin-angiotensin system during these
conditions remains unknown. Future research
may help to provide an answer to this
question, and to elucidate to what extent the
renin-angiotensin system may contribute to
beta-cell dysfunction in these diseases.
The systemic renin-angiotensin system (RAS)
is known to be of major importance for the
regulation of blood pressure [1, 2]. In recent
years, the existence of a local RAS in various
organs has also been demonstrated [3, 4, 5].
This implies that locally produced angiotensin
II (AT II) exerts local effects, a fact which has
been corroborated in several organs, e.g.
gonads [6], heart [7] and adrenals [8]. An
intrinsic RAS has also been demonstrated
both in the endocrine and exocrine pancreas
[9, 10, 11, 12]. Although much progress has
recently been made, the physiological
significance of the RAS in the endocrine
pancreas remains conjectural. Of interest in
this context is the accumulating data which
suggests a crucial role of hyperexpression of
angiotensinogen in essential hypertension (for
a review see [13]). The close relationship
between essential hypertension and type 2
diabetes [14, 15], and the beneficial effects of
ACE-inhibition for insulin release in many
hypertensive patients [16, 17, 18], underlines
the importance of increasing our
understanding of the physiological role of the
RAS in the pancreatic islets.
This review will focus on the RAS in the
endocrine pancreas. The morphological basis
and the current knowledge of physiological
functions in islets will be discussed. In
addition, the potential role of disturbances in
the islet RAS in diabetes mellitus and
hypertension will be addressed.
Current Basic Evidence of the Importance
of RAS
Presence of RAS-components in the
Angiotensinogen mRNA, angiotensinogen
protein, AT II and high affinity binding sites
for AT II have all been described in the
canine pancreas [9]. In dogs, AT II was the
most abundant RAS peptide, whereas
angiotensin III and angiotensin-(1-7) were
present in concentrations less than 20% of
that of AT II. The concentrations of these
three peptides in the canine pancreas were

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JOP – Journal of the Pancreas - - Vol.2, No. 1 January 2001
several times higher than those measured in
the blood. However, in the study by Chappell
et al. [9] neither angiotensin I nor renin
activity was detected in the pancreas. These
findings thereby question the existence of the
common processing pathway described in the
blood compartment and in other tissues [4].
angiotensinogen, renin and the AT II receptor
subtypes, AT1a, AT1b
and AT2
determined in the rat pancreas using reverse-
transcription PCR [11]. The presence of
angiotensinogen protein, a compulsory
component of an intrinsic RAS, was
demonstrated by Western blotting, and
localized by immunohistochemistry to the
epithelium of pancreatic ducts and
endothelium of blood vessels [11].
angiotensinogen in the pancreas of both rats
and dogs was low, and constituted only
approximately 2.5% of circulating
angiotensinogen concentrations [9, 11]. Using
the Northern blot technique, Campbell and
Habener were unable to detect
angiotensinogen mRNA in the rat pancreas in
an earlier study [3]. This discrepancy may be
explained by the lower sensitivity of Northern
blots. Interestingly, when using the Northern
blot technique, angiotensinogen mRNA could
be detected in all tumors and cell lines
derived from the radiation-induced rat
pancreatic islet cell line RIN-r [19, 20]. This
suggests that islets have a higher expression
of angiotensinogen than the exocrine
pancreas. However, it cannot be excluded that
it merely reflects the undifferentiated state of
these tumor cells [21]. The cellular co-
existence of the components of the RAS in
the exocrine and endocrine pancreas strongly
suggests the existence of a local RAS
generating intracellular AT II, which exerts
autocrine and paracrine functions. However, it
remains possible that intracellularly generated
AT II is synthesized through a renin-
independent pathway. For example, a study
by Hojima et al. [22] reported that both the
dog and rat pancreas contain kallikrein, i.e. an
enzyme capable of forming AT II directly
from its precursor angiotensinogen [23].
Since then, a number of serine proteases, all
of which are capable of generating AT II from
angiotensin I and angiotensinogen have been
described [24]. Some of these have also been
shown to be present in the pancreas [25]. In
addition, it is possible that locally formed
angiotensinogen is secreted and then
processed extracellularly to AT II by
circulating plasma renin [26]. Internalization
of the peptide ligand-receptor complex by the
high affinity binding sites present in the
pancreatic tissue would also be consistent
with the presence of AT II and the absence of
angiotensin I in the pancreas.
AT II immunoreactivity in the mouse
pancreas has been localized predominantly to
endothelial cells and epithelial cells of ducts
[27]. Less pronounced immunoreactivity for
AT II could, in that study, be discerned in
acinar cells and smooth muscle, whereas no
AT II immunoreactivity was detected in islet
cells [27]. In the canine pancreas, receptors
for AT II are found on endocrine, exocrine,
and vascular cells [9]. In the rat pancreas,
receptors for AT II are mainly located in
islets, and preferentially to the surface of
alpha- and delta-cells [10]. The majority of
binding sites in the canine pancreas are AT2
receptors, although ATreceptors can also be
seen [28]. In rodents similar numbers of AT1
and ATreceptors are found in the pancreas
[29]. In the human pancreas, the presence of
both ATreceptors and (pro)renin have been
demonstrated in islets [12]. ATreceptors are
located on beta-cells and endothelial cells,
whereas (pro)renin mRNA is confined to
blood vessels and reticular fibers within the
islets [12].
Physiological role of RAS in the endocrine
Binding sites for AT II in the rat pancreas
have been demonstrated, as mentioned above,
mainly on the surface of alpha- and delta-
cells, i.e. in the periphery of the islets [10].
Interestingly, it has been shown that AT II
receptors influence prostaglandin synthesis
[30, 31], which in turn may modulate the
secretion of insulin and glucagon. [32].
However, in isolated rat islet cells, AT II
affects neither insulin nor glucagon release
[33]. It should be kept in mind that studies on

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JOP – Journal of the Pancreas - - Vol.2, No. 1 January 2001
isolated cells may not accurately reflect
complex hormonal interactions seen in vivo.
It is possible that AT II modulates the
secretion of other regulatory pancreatic
hormones such as cholecystokinin, pancreatic
polypeptide or somatostatin, which then
influence alpha- or beta-cell function.
Moreover, the possible effects of the vascular
system on islet function is not evaluated in
such an in vitro system. To address the latter
question, enalaprilate, an inhibitor of ACE,
and saralasin, a non-selective AT II receptor
antagonist, were administered in vivo to rats,
and the effects on whole pancreatic and islet
blood flow were then determined. Both drugs
preferentially increased islet blood flow [34].
This finding suggests that islet microvessels
produce higher levels of AT II than those in
the exocrine pancreas, and therefore may be
more sensitive to ACE- or AT II receptor
inhibition. Moreover, islet blood flow seems,
under normal conditions, to be suppressed by
this locally produced AT II. Interestingly, in
support of these in vivo findings, recent
studies from me and my co-workers have
shown that islet capillary endothelial cells
express high amounts of ACE (unpublished
Experimental studies on the effects of the
angiotensin-system on insulin release were
made in a pancreas with an intact vascular
system by measuring insulin concentrations in
the effluents from isolated perfused rat
pancreata. In these preparations, enalaprilate
affected neither basal nor glucose-stimulated
insulin release, whereas AT II delayed the
first phase of insulin release in response to
glucose (Figure 1) [34]. The effect of AT II
was shown to be due to vasoconstriction, and
suggests a crucial role of intact islet blood
perfusion for maintenance of an adequate
insulin release.
Figure 1. Insulin concentrations in effluent medium
collected from perfused pancreata of male Sprague-
Dawley rats. The upper panel shows insulin secretion
in response to a 30-min period with 16.7 mmol/L D-
glucose (bar) added to the perfusion medium. The
lower panel shows insulin secretion in response to a
30-min period with 16.7 mmol/L D-glucose + 10
ng/mL angiotensin II (bar). Values represent means ±
SEM for 6-7 experiments.
Modified from [34].
The effects of ACE-inhibition on splanchnic
blood flow in humans is similar to that
observed in rats [35, 36]. Although no studies
in man have focused on the blood perfusion
of the pancreatic islets, it seems possible, in
view of the findings referred to above, that
AT II may be involved in the control of the
Interestingly, intravenous infusion of
angiotensin II in pressor doses (5.0 ng AT II x
x min
) suppressed both basal and
pulsatile insulin secretion in humans [37]. A
subpressor dose (1.0 ng AT II x kg
x min
also tended to suppress insulin secretion.

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JOP – Journal of the Pancreas - - Vol.2, No. 1 January 2001
After an oral glucose load, the insulinemic
response was significantly lower and the
significantly higher when AT II was infused
as compared to a placebo. Unfortunately, the
study design did not allow differentiating as
to whether the actions of AT II on insulin
secretion were a result of decreased blood
flow to the islets or if they were mediated via
AT II receptors on beta-cells.
Very scarce information exists on the
occurrence of RAS in transplanted pancreatic
islets. However, in recent experiments,
infusion of AT II in a dose that caused no
change in islet blood flow or vascular
conductance in native pancreatic rat islets,
caused a marked decrease in both blood flow
and vascular conductance in transplanted rat
islets [38]. This suggests that the blood flow
response to AT II in islet grafts differs from
that of native islets. In transplanted islets, a
chronic marked decrease in tissue oxygen
tension is seen after transplantation [39, 40].
Interestingly, it has also recently been shown
that chronic hypoxia causes a marked increase
in angiotensinogen, both at the gene and
protein levels, in the rat pancreas [41].
Increased expression of AT2- and AT1b-
receptors was also demonstrated, whereas no
changes in expression of mRNA expression
for AT1a occurred [41]. So far, no studies
have been conducted specifically on the RAS
in islets during hypoxia. Whether
upregulation of the RAS occurs secondary to
low oxygen tension levels in the grafted islets,
or merely is an effect of the implantation
organ (kidney), remains to be determined.
Future Basic Perspectives
Current knowledge on RAS in the endocrine
and exocrine pancreas has been obtained
mainly from morphological studies. Few
studies have addressed the functional role of
the RAS in the pancreas. In the future, it is
therefore important to expand the knowledge
on this in in-vivo systems, in view of the
marked vascular activity of the different RAS
components. Moreover, the regulation of the
RAS during different conditions and the
influence of disease, e.g. diabetes and
hypertension, are important to investigate.
The RAS in islets seems to be affected by
transplantion and the consequences of this for
graft function should be evaluated.
Knowledge of Actual Importance of RAS
in the Clinical Setting
The pancreatic islet RAS in diabetes mellitus
In patients treated with the ACE-inhibitor
ramipril due to a high risk of cardiovascular
events, a marked reduction in the incidence of
diabetes and development of diabetes
complications has been observed [42]. A
decreased diabetes incidence after treatment
with an ACE-inhibitor was also noted in the
Captopril Prevention Project (CAPP)
randomized trial [43]. It is well known that
type 2 diabetes often occurs together with
essential hypertension [14]. Moreover,
hypertension is a risk factor for the
subsequent development of type 2 diabetes
[15]. It has therefore been hypothesized that
some factor(s) common to hypertension and
diabetes may underlie the strong association
between these diseases. Peripheral insulin
resistance is commonly found in patients with
essential hypertension and type 2 diabetes
[44]. However, it seems that type 2 diabetes
does not develop as long as the pancreatic
beta-cells can secrete sufficient quantities of
insulin to maintain normal glucose
homeostasis [45]. Interestingly, several
studies in hypertensive patients receiving
long-term treatment with ACE-inhibitors,
have described an increased initial phase
insulin peak in response to intravenous
glucose administration [16, 17] or oral
glucose [18]. Whether this improved insulin
secretion response reflects vascular effects in
the islets, or is mediated via AT II receptors
on beta-cells remains to be determined.
However, so far no studies have described the
presence of AT II receptors on the surface of
beta-cells, nor have any effects of AT II on
isolated beta-cells or islets been found (cf.
above). By comparison, profound effects of
AT II on insulin release, secondary to
impaired islet blood flow, has been observed
in an experimental study conducted in rats
[38]. It may be speculated that hyperactivity

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JOP – Journal of the Pancreas - - Vol.2, No. 1 January 2001
of the angiotensin system in islet vasculature
impairs insulin release. Indeed, in the diabetic
state, increased ACE-concentrations occur in
the mesenteric vasculature, at least in animals
responsiveness to AT II in diabetic patients
has also been observed [47, 48]. In addition,
changes in vascular ACE seem to occur in
various models of hypertension [49]. In
spontaneously hypertensive rats (SHR), the
renin-angiotensin system exerts a tonic
vasoconstrictor action on the mesenteric
vasculature [50].
Future Clinical Perspective
Even though ACE-inhibition has shown
beneficial effects on islet function in several
clinical studies, the mechanism behind this
remains to be elucidated. The involvement of
the islet RAS for the close correlation that
exists between hypertension and type 2
diabetes in the clinical setting, emerges as a
potential link. In the future, it will therefore
be important to investigate more closely the
role of the islet RAS in human diabetes and
hypertension, especially with regard to
potential circulatory effects.
Key words Islets of Langerhans; Angiotensin
II, Insulin (secretion); Microcirculation
Abbreviations AT II: angiotensin II
Acknowledgements Own work referred to in
this paper was financially supported by grants
from the Swedish Medical Research Council
(17X-109), the Swedish-American Diabetes
Research Program jointly funded by the
Juvenile Diabetes Foundation International
and the Wallenberg Foundation, the Juvenile
Diabetes Foundation International, the
Swedish Diabetes Association, Svenska
Barndiabetesfonden, the Novo Research
Fund, the Family Ernfors Fund, the Magnus
Bergvall Foundation, the Harald Jeansson and
Harald and Greta Jeansson Foundation.
Per-Ola Carlsson
Department of Medical Cell Biology
Biomedical Center
Husargatan 3, Box 571
SE-751 23 Uppsala
Phone: +46-18-4714.425
Fax: +46-18-556.401
E-mail address:
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